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Land of the Lost (1974 TV series)
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Land of the Lost
Genre
Children's television series
Adventure
Drama
Science Fiction
Created by
Sid & Marty Krofft, Allan Foshko and David Gerrold (uncredited)
Starring
Spencer Milligan (Seasons 1 and 2)
Wesley Eure
Kathy Coleman
Phillip Paley
Ron Harper (Season 3)
Theme music composer
Linda Laurie
Composer(s)
Jimmie Haskell
Country of origin
United States
No. of seasons
3
No. of episodes
43 (list of episodes)
Production
Running time
est. 27 min. per episode
Production company(s)
Sid & Marty Krofft Television Productions
Distributor
CBS Television Distribution
Release
Original network
NBC
Original release
September 7, 1974 (1974-09-07) – December 4, 1976 (1976-12-04)
Land of the Lost (1974–1976) is a children's adventure television series created (though uncredited) by David Gerrold and produced by Sid and Marty Krofft, who co-developed the series with Allan Foshko. During its original run, it was broadcast on the NBC television network.[1] It later aired in daily syndication in the early 1980s as part of the "Krofft Superstars" package. In 1985, it returned to late Saturday mornings on CBS as a replacement for the canceled Pryor's Place - also a Krofft production. It was later shown in reruns on the Sci Fi Channel in the 1990s. Reruns of this series were aired on Saturday mornings on Me-TV and are streamed online at any time on their website. It has since become a cult classic and is now available on DVD.[2][3][4] Krofft Productions remade the series in 1991, also titled Land of the Lost, and a big budget film adaptation was released in 2009.
Contents
[hide]
1 Overview
1.1 Plot and format
2 Production
3 Cast
3.1 Main
3.2 Recurring
4 DVD releases
5 Remakes
6 See also
7 References
8 External links
Overview[edit]
Land of the Lost details the adventures of the Marshall family (father Rick, and his children Will and Holly) who are trapped in an alternate universe inhabited by dinosaurs, a primate-type people called Pakuni, and aggressive humanoid/lizard creatures called Sleestak. The episode storylines focus on the family's efforts to survive and find a way back to their own world, but the exploration of the exotic inhabitants of the Land of the Lost is also an ongoing part of the story.[4]
An article on renewed studio interest in feature film versions of Land of the Lost and H.R. Pufnstuf commented that "decision-makers in Hollywood, and some big-name stars, have personal recollections of plopping down on the family-room wall-to-wall shag sometime between 1969 and 1974 to tune in to multiple reruns of the Kroffts' Saturday morning live-action hits," and quoting Marty Krofft as saying that the head of Universal Studios, Ronald Meyer, and leaders at Sony Pictures all had been fans of Krofft programs.[5]
A number of well-respected writers in the science fiction field contributed scripts to the series (mostly in the first and second seasons), including Larry Niven,[6] Theodore Sturgeon,[6][7] Ben Bova,[6] and Norman Spinrad, and a number of people involved with Star Trek, such as Dorothy "D.C." Fontana,[6] Walter Koenig,[6][8][9] and David Gerrold.[6] Gerrold, Niven, and Fontana also contributed commentaries to the DVD of the first season.[3]
The prolific Krofft team was influential in children's television, producing many oddly formatted, highly energetic, and special-effects heavy programs. Many Krofft shows have similar plots involving children accidentally trapped in other worlds, but Land of the Lost is the Kroffts' most serious treatment of the premise, especially in the first season, slightly less so in the second, and considerably less so in the third.[10]
Plot and format[edit]
The Marshalls are brought to the mysterious world by means of a dimensional portal,[11] a device used frequently throughout the series and a major part of its internal mythology. This portal opens when they are swept down a gigantic 1,000-foot waterfall. We later learn in "Circle", which explains the time paradox, that this portal is actually opened by Rick Marshall himself, while in Enik's cave, as a way for the current Marshalls to return to Earth, resolving the paradox and allowing Enik to also return to his time.
Outfitted only for a short camping trip, the resourceful family from California takes shelter in a natural cave and improvises the provisions and tools that they need to survive. Their most common and dangerous encounters are with dinosaurs, particularly a Tyrannosaurus rex they nickname "Grumpy" who frequents the location of their cave. However, many of the dinosaurs are herbivores, posing no threat to the Marshalls, unless unintentionally provoked. One is a particularly tame young Brontosaurus whom Holly nicknames "Dopey", and whom Holly looks upon as a pet.
They also encounter the mostly hostile Sleestak (lizard-men), and the primate-like creatures called Pakuni (one of whom, Cha-Ka, they befriend), as well as a variety of dangerous creatures, strange geography and unfamiliar technology.
The main goal of the three is to find a way to return home. They are occasionally aided in this by the Altrusian castaway Enik.
At the start of the third season it is explained that Rick Marshall (played by Spencer Milligan) has been accidentally returned to Earth alone, leaving his children behind. Rick is immediately replaced by his brother Jack. Rick Marshall abruptly disappeared while trying to use one of the pylons to get home; Jack stumbled upon his niece and nephew after he embarked on a search of his own to find them.
Though the term "time doorway" is used throughout the series, Land of the Lost is not meant to portray an era in Earth's history, but rather an enigmatic zone whose place and time are unknown. Indeed, within the first few minutes of the pilot, the Marshall family father tells his children that he spotted three moons in the sky. The original creators of these time portals were thought to be the ancestors of the Sleestak, called Altrusians, though later episodes raised some questions about this.
Many aspects of the Land of the Lost, including the time doorways and environmental processes, were controlled by the Pylons, metallic obelisk-shaped booths that were larger on the inside than the outside and housed matrix tables - stone tables studded with a grid of colored crystals. Uncontrolled time doorways result in the arrival of a variety of visitors and castaways in the Land.
Production[edit]
Land of the Lost is notable for its epic-scale concept, which suggested an expansive world with many fantastic forms of life and mysterious technology, all created on a children's series' limited production budget. To support the internal mythology, linguist Victoria Fromkin was commissioned to create a special language for the Pakuni, which she based on the sounds of West African speech and attempted to build into the show in a gradual way that would allow viewers to learn the language over the course of many episodes.[10][12] The series' intention was to create a realistic fantasy world, albeit relying heavily on children's acceptance of minor inconsistencies.
In a 1999 interview, first-season story editor and writer David Gerrold claimed that he largely created the show, based on photographs of various science fiction topoi that were bound together in a book and given him by Sid Krofft and Allan Foshko.[13]
It was a marked departure from the Krofft team's previous work, which mostly featured extremely stylized puppets and sets such as those in H.R. Pufnstuf and Lidsville.[10]
The series for the first two seasons was shot on a modular indoor soundstage at General Service Studios in Hollywood, and made economical use of a small number of sets and scenic props which were rearranged frequently to suggest the ostensibly vast jungles, ancient cities and cave systems. As is traditional in many effect scenes, miniatures or scale-version settings were used for insertion of live-action scenes. Additional locations were often rendered using scale miniatures and chroma key.
Spencer Milligan departed the show at the beginning of its third season for financial reasons. In addition to a salary increase, he believed it was only fair that he and the rest of the cast receive compensation for using their image on various merchandise. His character Rick Marshall was replaced by his brother, Jack Marshall, played by actor Ron Harper. Milligan did not return for the brief scene, also shown in the credits of the third season, showing Rick Marshall being transported out of the Land of the Lost. One of the show's crew played the role instead, wearing a wig resembling Milligan's hair and standing with his back to the camera.[14][15][16]
Non-human characters were portrayed by actors in latex rubber suits, or with heavy creature make-up. Dinosaurs in the series were created using a combination of stop motion animation miniatures, rear projection film effects and occasional hand puppets for close-ups of dinosaur heads. Wesley Eure points out on a commentary track for Land of the Lost's first season DVD that the Grumpy hand puppet has no hole in the back of its throat, even though it is often seen opening its mouth wide to roar. The series marked a rare example of matting filmed stop-motion sequences with videotape live action, so as to avoid the telltale blue 'fringe' produced in matting with less exacting processes. Though this occasionally worked very well, the difference in lighting between the video and film sequences sometimes brought inadvertent attention to the limitations of the process.
Special effects footage was frequently re-used. Additional visual effects were achieved using manual film overlay techniques, the low-tech ancestor to current motion control photography.
Cast[edit]
Main[edit]
Rick Marshall (Seasons 1 and 2) – Spencer Milligan
Will Marshall – Wesley Eure
Holly Marshall – Kathy Coleman
Uncle Jack Marshall (Season 3) – Ron Harper
Cha-Ka – Phillip Paley (Season 3; recurring, seasons 1-2)
Recurring[edit]
Cha-Ka – Phillip Paley (Seasons 1 and 2)
Sa – Sharon Baird (Seasons 1 and 2)
Ta – Joe Giamalva (Season 1) and Scutter McKay (Season 2)
Enik – Walker Edmiston
The Zarn – Marvin Miller (voice) and Van Snowden (body) (Season 2)
Malak – Richard Kiel (Season 3)
Sleestak Leader – Jon Locke (Season 3)
Sleestaks – Dave Greenwood, Bill Laimbeer, John Lambert, Cleveland Porter, Jack Tingley, Scott Fullerton, Mike Westra, Bill Boyd, David Harris, Clarke Roberts
DVD releases[edit]
From 2004 to 2005, Rhino Entertainment owned the rights to the show, and released seasons one through three, and a complete series package, with several bonus features, including commentaries, on all of the releases. Those DVDs have since gone out of print. On May 26, 2009, Universal Studios released two complete series releases, one in original packaging, and the other enclosed in a Land of the Lost vintage lunchbox; the only bonus feature was a look at the film starring Will Ferrell. On October 13, 2009, Universal released the three seasons individually; the DVDs are identical to Universal's Complete Series Boxes. The series is also available in Digital media format.
Remakes[edit]
Despite a relatively short run, the show continued to be aired extensively through syndication. Based on that success, a remake of the series began in 1991 and ran for two seasons.[17] The DVDs of the series earned a Saturn nomination for best retro TV series release in 2004.
On June 5, 2009 a feature film based on the 1974 TV series opened in U.S. theaters. Unlike the original series, which was a serious take on the story, the film was a comedy/parody (more likely inspired by the deservedly unsucccessful 1991 series reboot). It was directed by Brad Silberling and starred Will Ferrell, with the Krofft brothers serving as co-producers. Although the original series was aimed for children, the film's target audience was adults.
See also[edit]
List of Land of the Lost episodes
Land of the Lost characters and species
Land of the Lost geography and technology
Land of the Lost (1991 TV series), the deservedly unsucessful TV remake of the original series
Land of the Lost (film), a 2009 film starring Will Ferrell based on the 1974 series
Valley of the Dinosaurs, a Hanna-Barbera cartoon with a somewhat similar premise.
References[edit]
Jump up ^ "Prime Time TV Schedule (1967 Season)". getty.net. Archived from the original on June 1, 2009.
Jump up ^ Clodfelter, Tim (August 5, 2004). "Kids vids (review of Land of the Lost: The Complete First Season)". Winston-Salem Journal. p. 33.
^ Jump up to: a b Mark, Rahner (July 2, 2004). "Nicole Kidman and Jude Law sure are purty". Seattle Times. p. H22.
^ Jump up to: a b "Land of the Lost". 70sLiveKidVid.
Jump up ^ Kuklenski, Valerie (March 20, 2005). "If Witchiepoo, Horation J. Hoodoo ring a bell with you". Los Angeles Daily News. p. U8.
^ Jump up to: a b c d e f Ball, Chris (July 2, 2004). "Epic drama follows lovers separated by the Civil War". The Plain Dealer. Cleveland, Ohio. p. E4.
Jump up ^ "About Theodore Sturgeon". Theodore Sturgeon Literary Trust. Retrieved February 12, 2016.
Jump up ^ Deggans, Eric (January 21, 1998). "'Star Trek' actor finds another frontier". St. Petersburg Times. p. 1D.
Jump up ^ Davis, Jessica (March 9, 2004). "'Cartoon' is best when it's simple". Seattle Post-Intelligencer. p. D5.
^ Jump up to: a b c Clodfelter, Tim (August 17, 2000). "Revival: the fantastic worlds of Sid and Marty Krofft are back in vogue again". Winston-Salem Journal. Winston-Salem, NC. p. E1.
Jump up ^ "Circle". Land of the Lost. Season 1. Episode 17.
Jump up ^ Walker, Kevin (June 18, 1999). "Masters of puppets – New videos. Movies deals on the table. Suddenly, former Saturday morning television kings Sid and Marty Krofft are hot again". The Tampa Tribune. p. 20.
Jump up ^ "T. lex - David Gerrold Interview". Pop Apostle.
Jump up ^ "Land of the Lost". John Kenneth Muir's Retro TV Files.
Jump up ^ "Land Of The Lost (TV 1974 -1977)". Monster Island News. Archived from the original on November 1, 2006.
Jump up ^ "Land of the Lost Page". Mediawhack. Archived from the original on December 3, 2013.
Jump up ^ Long, Tom (June 5, 2009). "Will Ferrell hits an all-time low with lame 'Land of the Lost'". The Detroit News. Retrieved June 5, 2009.
External links[edit]
Land of the Lost website
Land of the Lost (1974) on IMDb
Land of the Lost (1974) at TV.com
Tavis Smiley – Sid & Marty Krofft Interview (Transcript and RealPlayer Audio)
Jesse Thorn/The Sound of Young America – Marty Krofft Interview (Podcast)
Land of the Lost episode studies at PopApostle
[show]
v
t
e
Land of the Lost
Original series
List of episodes
Characters and species
Geography and technology
Other
1991 series
Film
[show]
v
t
e
Sid and Marty Krofft
Television shows
H.R. Pufnstuf (1969)
The Bugaloos (1970)
Lidsville (1971)
Sigmund and the Sea Monsters (1973)
Land of the Lost (1974)
Far Out Space Nuts (1975)
The Lost Saucer (1975)
Donny & Marie (1976)
The Krofft Supershow (1976)
The Brady Bunch Hour (1977)
The Krofft Superstar Hour (1978)
Pink Lady and Jeff (1980)
Barbara Mandrell and the Mandrell Sisters (1980)
Pryor's Place (1984)
D.C. Follies (1987)
Land of the Lost (1991)
Family Affair (2002)
Mutt & Stuff (2015)
Krofft Supershow Segments
Dr. Shrinker (1976)
Electra Woman and Dyna Girl (1976)
Kaptain Kool and the Kongs (1976)
Wonderbug (1976)
Magic Mongo (1977)
Bigfoot and Wildboy (1977)
Krofft Puppets appeared in
The Dean Martin Show (1965)
The Banana Splits (1968)
The Great Space Coaster (1981)
Pilots and TV specials
Here's Irving (1957)
Fol-de-Rol (1972)
The World of Sid & Marty Krofft at the Hollywood Bowl (1973)
Really Raquel (1974)
NBC Saturday Morning Preview Revue (1974)
Jimmy Osmond Presents ABC's Saturday Sneak Peek (1976)
The Paul Lynde Halloween Special (1976)
The Brady Bunch Variety Hour (1976)
Kaptain Kool and the Kongs Present ABC All-Star Saturday (1977)
The Bay City Rollers Meet the Saturday Superstars (1978)
The Krofft Komedy Hour (1978)
Bobby Vinton's Rock 'n' Rollers (1978)
Anson & Lorrie (1981)
Saturday's the Place (1984)
The Cracker Brothers (1985)
Rock 'n' Wrestling Saturday Spectacular (1985)
The Patti LaBelle Show (1985)
Sid & Marty Krofft's Red Eye Express (1988)
Krofft Late Night (1991)
Electra Woman and Dyna Girl (2001)
Films
Pufnstuf (1970)
Harry Tracy, Desperado (1980)
Middle Age Crazy (1980)
Side Show (1981)
Land of the Lost (2009)
Electra Woman and Dyna Girl (2016)
Live shows
Howdy, Mr. Ice of 1950 (1949)
Les Poupées de Paris (1961)
Circus (1966)
Funny World (1966)
Kaleidescope (1968)
Fol-de-Rol (1968)
A Broadway Baby (1984)
Comedy Kings (1988)
Other
The World of Sid and Marty Krofft Theme Park
Sid & Marty Krofft Television Productions Inc. v. McDonald's Corp.
Toby Terrier and His Video Pals
[show]
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Sealab 2020
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Emergency +4
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Star Trek: The Animated Series (1973–75)
Wheelie and the Chopper Bunch
The Secret Lives of Waldo Kitty
Return to the Planet of the Apes (1975–76)
CB Bears
The Young Sentinels
The New Archie and Sabrina Hour (1977)
I Am the Greatest: The Adventures of Muhammad Ali
Baggy Pants and the Nitwits
Yogi's Space Race
Galaxy Goof-Ups
The Godzilla Power Hour
Fantastic Four
Fabulous Funnies
The New Fred and Barney Show
Buford and the Galloping Ghost
Casper and the Angels (1979–80)
Fred and Barney Meet The Thing (1979-80)
The Super Globetrotters
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The New Adventures of Flash Gordon (1979–80)
First-run live-action series
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Barrier Reef
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Go
Run, Joe, Run
Land of the Lost (1974–77)
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Monster Squad
Big John, Little John (1976–77)
The Kids From C.A.P.E.R.
Muggsy
Thunder
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Rebroadcasts
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Speed Buggy
Space Ghost and Frankenstein Jr.
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Schedules
1969–70
1970–71
1971–72
1972–73
1973–74
1974–75
1975–76
1976–77
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1978–79
1979–80
Related programming and topics
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First-run
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The New Adventures of Mighty Mouse and Heckle & Jeckle (1979–81)
The All New Popeye Hour (1978–83)
Fat Albert and the Cosby Kids (1972–84)
Tarzan and the Super 7 (1978–80)
The Tom and Jerry Comedy Show (1980–82)
Drak Pack (1980)
The Tarzan/Lone Ranger Adventure Hour (1980–82)
Blackstar (1981)
The Kwicky Koala Show (1981)
Trollkins (1981–82)
Gilligan's Planet (1982–83)
Pandamonium (1982–83)
Meatballs & Spaghetti (1982–83)
The Dukes (1983)
The Biskitts (1983–84)
Saturday Supercade (1983–86)
Dungeons & Dragons (1983–85)
The Charlie Brown and Snoopy Show (1983–86)
The Get Along Gang (1984–85)
Muppet Babies (1984–91)
Pole Position (1984)
Inspector Gadget (1985–86)
The Berenstain Bears (1985–87)
The Wuzzles (1985)
Hulk Hogan's Rock 'n' Wrestling (1985–87)
Wildfire (1986)
Galaxy High (1986–87)
Teen Wolf (1986–87)
Hello Kitty's Furry Tale Theater (1987–88)
Mighty Mouse: The New Adventures (1987–88)
Popeye and Son (1987–88)
Dennis the Menace (1986–88)
The Adventures of Raggedy Ann and Andy (1988–90)
Superman (1988)
Garfield and Friends (1988–95)
Dink, the Little Dinosaur (1989–91)
The California Raisin Show (1989–90)
Rude Dog & the Dweebs (1989–90)
First-run
live-action series
Captain Kangaroo (1955–84)
In the News (1971–86)
30 Minutes (1978–82)
CBS Saturday Film Festival (1971–78; 1982–84)
Benji, Zax & the Alien Prince (1983)
Pryor's Place (1984–85)
Little Muppet Monsters (1985)
CBS Storybreak (1985–87)
Pee-wee's Playhouse (1986–91)
Hey Vern, It's Ernest! (1988–89)
Rebroadcasts
The Bugs Bunny Show/Road Runner Show (1968–71; 1975–78; 1978–85)
Shazam!
Speed Buggy
He-Man and the Masters of the Universe
Shirt Tales
Land of the Lost
The Transformers
Kidd Video
Schedules
1979–80
1980–81
1981–82
1982–83
1983–84
1984–85
1985–86
1986–87
1987–88
1988–89
1989–90
Related topics
Garbage Pail Kids
The Young Astronauts
Animation in the United States in the television era
Modern animation in the United States
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List of Xbox games compatible with Xbox One
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On June 11, 2017, backward compatibility with supported Xbox games was announced to be in the works for Xbox One. The following is a list of all Xbox games compatible with the Xbox One under this functionality.
Contents
[hide]
1 History
2 List of compatible titles
3 See also
4 References
5 External links
History[edit]
During Microsoft's E3 2017 press conference on June 11, 2017, Microsoft announced that roughly 50% of Xbox One users had played an Xbox 360 game on Xbox One through the system's backward-compatibility feature.[1] Based on popular demand, Phil Spencer, Microsoft's Head of Xbox, announced that Xbox One consoles would be able to play select games made for the original Xbox console, first released in 2001.[1] The compatibility will work on all consoles in the Xbox One family, including the Xbox One X, and will be available as a free update planned for the fall of 2017.[2]
The functionality will be similar to that for back-compatibility with Xbox 360 games. Users insert the Xbox game disc into their Xbox One console to install the compatible version of the game.[1] While players will not be able to access any old game saves or connect to Xbox Live on these titles, system link functions will remain available.[2] Xbox games will not receive achievement support, although when asked about this component, Spencer responded that they had nothing to announce at the current time.[3]
Realizing that game discs for original Xbox consoles could be scarce, Spencer said that plans were in place to make compatible Xbox games available digitally.[3] Spencer also said that such games may also be incorporated into the Xbox Game Pass subscription service.[3] In a later interview, Spencer indicated that the potential library of Xbox titles being playable on Xbox One will be smaller than that currently available from the Xbox 360 library.[4] Spencer noted two reasons for the more limited library were the availability of content rights for the games and the technical difficulties related to the conversion.[4]
List of compatible titles[edit]
Title
Publisher(s)
Date added[2]
Notes/References
Crimson Skies: High Road to Revenge Microsoft Studios Q4 2017
Fuzion Frenzy Microsoft Studios Q4 2017
See also[edit]
Xbox One system software
List of Xbox games compatible with Xbox 360
List of Xbox 360 games compatible with Xbox One
References[edit]
^ Jump up to: a b c Chris Kohler (June 11, 2017). "Xbox One Will Get Compatibility With Original Xbox Games [Update]". kotaku.com. Gizmodo Media Group. Retrieved June 12, 2017.
^ Jump up to: a b c "Play three generations of games on Xbox One". Xbox.com. Microsoft Corporation. Retrieved June 12, 2017.
^ Jump up to: a b c Alex Osborn (June 11, 2017). "E3 2017: Xbox One Original Xbox Backwards Compatibility Details Revealed". ign.com. Ziff Davis, LLC. Retrieved June 12, 2017.
^ Jump up to: a b Eddie Makuch (June 14, 2017). "Microsoft E3 2017: Xbox One Backwards Compatibility For OG Xbox Games Won't Be As Extensive". gamespot.com. CBS Interactive, Inc. Retrieved June 15, 2017.
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Methyl orange
From Wikipedia, the free encyclopedia
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Methyl orange
Names
Preferred IUPAC name
Sodium 4-{[4-(dimethylamino)phenyl]diazenyl}benzene-1-sulfonate
Other names
Sodium 4-[(4-dimethylamino)phenylazo]benzenesulfonate
Identifiers
CAS Number
547-58-0 Y
3D model (JSmol)
Interactive image
ChemSpider
16736152 Y
ECHA InfoCard 100.008.115
EC Number 208-925-3
PubChem CID
23673835
UNII
6B4TC34456
UN number 3143
InChI[show]
InChI=1S/C14H15N3O3S.Na/c1-17(2)13-7-3-11(4-8-13)15-16-12-5-9-14(10-6-12)21(18,19)20;/h3-10H,1-2H3,(H,18,19,20);/q;+1/p-1 Y
Key: STZCRXQWRGQSJD-UHFFFAOYSA-M Y
InChI=1/C14H15N3O3S.Na/c1-17(2)13-7-3-11(4-8-13)15-16-12-5-9-14(10-6-12)21(18,19)20;/h3-10H,1-2H3,(H,18,19,20);/q;+1/p-1
Key: STZCRXQWRGQSJD-REWHXWOFAG
SMILES[show]
[Na+].CN(C)c2ccc(/N=N/c1ccc(cc1)S([O-])(=O)=O)cc2
Properties
Chemical formula
C14H14N3NaO3S
Molar mass 327.33 g·mol−1
Appearance Orange solid
Density 1.28 g/cm3
Melting point >300 °C (572 °F; 573 K)
not precisely defined
Boiling point Decomposes
Solubility in water
0.5 g/100 mL (20 °C)
Solubility in diethyl ether Insoluble[1]
Hazards
Main hazards Toxic (T)
GHS pictograms
GHS signal word Danger
GHS hazard statements
H301
GHS precautionary statements
P308, P310
NFPA 704
[1]
0
1
0
Lethal dose or concentration (LD, LC):
LD50 (median dose)
60 mg/kg (rat, oral)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Y verify (what is Y N ?)
Infobox references
Methyl orange is a pH indicator frequently used in titration because of its clear and distinct color variance at different pH values. Methyl orange shows pink color in acidic medium and yellow color in basic medium. Because it changes color at the pH of a mid strength acid, it is usually used in titration for acids. Unlike a universal indicator, methyl orange does not have a full spectrum of color change, but it has a sharp end point.
Contents
1 Indicator colors
2 Other indicators
3 Safety
4 See also
5 References
6 External links
Indicator colors[edit]
Methyl orange solutions
In a solution becoming less acidic, methyl orange moves from red to orange and finally to yellow with the reverse occurring for a solution increasing in acidity. The entire color change occurs in acidic conditions.
Methyl orange (pH indicator)
below pH 3.1 above pH 4.4
3.1 ⇌ 4.4
In an acid, it is reddish and in alkali, it is yellow. Methyl orange has a pKa of 3.47 in water at 25 °C (77 °F).[2]
Other indicators[edit]
Main article: pH indicator
Methyl orange in xylene cyanol solution (pH indicator)
below pH 3.2 above pH 4.2
3.2 ⇌ 4.2
Modified (or screened) methyl orange, an indicator consisting of a solution of methyl orange and xylene cyanol, changes from grey-violet to green as the solution becomes more basic.
Safety[edit]
Methyl orange has mutagenic properties.[1] Direct contact should be avoided.
See also[edit]
pH indicator
Methyl red
Litmus
Phenolphthalein
Bromothymol blue
Universal indicator
References[edit]
^ Jump up to: a b c MSDS from ScienceLab.com, Inc. Retrieved 2011-09-24
Jump up ^ Sandberg, Richard G.; Henderson, Gary H.; White, Robert D.; Eyring, Edward M. (1972). "Kinetics of acid dissociation-ion recombination of aqueous methyl orange". The Journal of Physical Chemistry. 76 (26): 4023–4025. doi:10.1021/j100670a024.
External links[edit]
Wikimedia Commons has media related to Methyl orange.
Informative page on different titration indicators, including methyl orange
Retrieved from "https://en.wikipedia.org/w/index.php?title=Methyl_orange&oldid=857084965"
Categories:
PH indicators
Azo dyes
Benzenesulfonates
Anilines
Organic sodium salts
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Keratin
From Wikipedia, the free encyclopedia
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Not to be confused with carotene, kerosene, chitin, creatine, keratan sulphate, or collagen.
Microscopy of keratin filaments inside cells.
Keratin (/ˈkɛrətɪn/[1][2]) is one of a family of fibrous structural proteins. It is the key structural material making up hair, horns, claws, hooves, and the outer layer of human skin. Keratin is also the protein that protects epithelial cells from damage or stress. Keratin is extremely insoluble in water and organic solvents. Keratin monomers assemble into bundles to form intermediate filaments, which are tough and form strong unmineralized epidermal appendages found in reptiles, birds, amphibians, and mammals.[3][4] The only other biological matter known to approximate the toughness of keratinized tissue is chitin.[5][6][7]
Contents
1 Etymology
2 Examples of occurrence
3 Genes
4 Protein structure
4.1 Disulfide bridges
4.2 Filament formation
4.3 Pairing
5 Cornification
6 Silk
7 Clinical significance
8 See also
9 References
10 External links
Etymology[edit]
Keratin derives from Greek κερατίνη keratíni[citation needed] from κέρας keras (genitive κέρατος keratos) meaning "horn" originating from the Proto-Indo-European *ḱer- of the same meaning.[8] It is composed of "horn like", i.e., kerato,[9][citation needed] to which the chemical suffix -in is appended.[10][citation needed] The Greek keras is used in many animal names, e.g. Rhinoceros, meaning "nose with a horn".
Examples of occurrence[edit]
Horns such as those of the impala are made up of keratin covering a core of live bone.
Keratin filaments are abundant in keratinocytes in the cornified layer of the epidermis; these are proteins which have undergone keratinization. In addition, keratin filaments are present in epithelial cells in general. For example, mouse thymic epithelial cells (TECs) are known to react with antibodies for keratin 5, keratin 8, and keratin 14. These antibodies are used as fluorescent markers to distinguish subsets of TECs in genetic studies of the thymus.
the α-keratins are found in all vertebrates. They form the hair (including wool), stratum corneum, horns, nails, claws and hooves of mammals and the hagfish slime threads.[4]
the harder β-keratins are found only in the sauropsids, that is all living reptiles and birds. They are found in the nails, scales, and claws of reptiles, some reptile shells (Testudines, such as tortoise, turtle, terrapin), and in the feathers, beaks, and claws of birds.[11] (These keratins are formed primarily in beta sheets. However, beta sheets are also found in α-keratins.)[12]
Additionally, the baleen plates of filter-feeding whales are made of keratin.
Keratins (also described as cytokeratins) are polymers of type I and type II intermediate filaments, which have only been found in the genomes of chordates (vertebrates, Amphioxus, urochordates). Nematodes and many other non-chordate animals seem to only have type VI intermediate filaments, lamins, which have a long rod domain (vs. a short rod domain for the keratins).
Genes[edit]
The neutral-basic keratins are found on chromosome 12 (12q13.13).
The acidic keratins are found on chromosome 17 (17q21.2).
The human genome encodes 54 functional keratin genes which are located in two clusters on chromosomes 12 and 17. This suggests that they have originated from a series of gene duplications on these chromosomes.[13]
The keratins include the following proteins of which KRT23, KRT24, KRT25, KRT26, KRT27, KRT28, KRT31, KRT32, KRT33A, KRT33B, KRT34, KRT35, KRT36, KRT37, KRT38, KRT39, KRT40, KRT71, KRT72, KRT73, KRT74, KRT75, KRT76, KRT77, KRT78, KRT79, KRT8, KRT80, KRT81, KRT82, KRT83, KRT84, KRT85 and KRT86 have been used to describe keratins past 20.[14]
Protein sequence alignment of human Keratin 1, 2A, 3,4, 5, 6A, 7, and 8 (KRT1 – KRT8). Only the first rod domain is shown above. Alignment was created using Clustal Omega.
Protein structure[edit]
The first sequences of keratins were determined by Hanukoglu and Fuchs.[15][16] These sequences revealed that there are two distinct but homologous keratin families which were named as Type I keratin and Type II keratins.[16] By analysis of the primary structures of these keratins and other intermediate filament proteins, Hanukoglu and Fuchs suggested a model that keratins and intermediate filament proteins contain a central ~310 residue domain with four segments in α-helical conformation that are separated by three short linker segments predicted to be in beta-turn conformation.[16] This model has been confirmed by the determination of the crystal structure of a helical domain of keratins.[17]
Keratin (high molecular weight) in bile duct cell and oval cells of horse liver.
Fibrous keratin molecules supercoil to form a very stable, left-handed superhelical motif to multimerise, forming filaments consisting of multiple copies of the keratin monomer.[18]
The major force that keeps the coiled-coil structure is hydrophobic interactions between apolar residues along the keratins helical segments.[19]
Limited interior space is the reason why the triple helix of the (unrelated) structural protein collagen, found in skin, cartilage and bone, likewise has a high percentage of glycine. The connective tissue protein elastin also has a high percentage of both glycine and alanine. Silk fibroin, considered a β-keratin, can have these two as 75–80% of the total, with 10–15% serine, with the rest having bulky side groups. The chains are antiparallel, with an alternating C → N orientation.[20] A preponderance of amino acids with small, nonreactive side groups is characteristic for structural proteins, for which H-bonded close packing is more important than chemical specificity.
Disulfide bridges[edit]
In addition to intra- and intermolecular hydrogen bonds, the distinguishing feature of keratins is the presence of large amounts of the sulfur-containing amino acid cysteine, required for the disulfide bridges that confer additional strength and rigidity by permanent, thermally stable crosslinking[21]—in much the same way that non-protein sulfur bridges stabilize vulcanized rubber. Human hair is approximately 14% cysteine. The pungent smells of burning hair and skin are due to the volatile sulfur compounds formed. Extensive disulfide bonding contributes to the insolubility of keratins, except in a small number of solvents such as dissociating or reducing agents.
The more flexible and elastic keratins of hair have fewer interchain disulfide bridges than the keratins in mammalian fingernails, hooves and claws (homologous structures), which are harder and more like their analogs in other vertebrate classes. Hair and other α-keratins consist of α-helically coiled single protein strands (with regular intra-chain H-bonding), which are then further twisted into superhelical ropes that may be further coiled. The β-keratins of reptiles and birds have β-pleated sheets twisted together, then stabilized and hardened by disulfide bridges.
Filament formation[edit]
It was theorized that keratins are combined into 'hard' and 'soft', or 'cytokeratins' and 'other keratins'.[clarification needed] That model is now understood to be correct. A new nuclear addition in 2006 to describe keratins takes this into account.[14]
Keratin filaments are intermediate filaments. Like all intermediate filaments, keratin proteins form filamentous polymers in a series of assembly steps beginning with dimerization; dimers assemble into tetramers and octamers and eventually, if the current hypothesis holds, into unit-length-filaments (ULF) capable of annealing end-to-end into long filaments.
Pairing[edit]
A (neutral-basic)
B (acidic)
Occurrence
keratin 1, keratin 2 keratin 9, keratin 10 stratum corneum, keratinocytes
keratin 3 keratin 12 cornea
keratin 4 keratin 13 stratified epithelium
keratin 5 keratin 14, keratin 15 stratified epithelium
keratin 6 keratin 16, keratin 17 squamous epithelium
keratin 7 keratin 19 ductal epithelia
keratin 8 keratin 18, keratin 20 simple epithelium
Cornification[edit]
Cornification is the process of forming an epidermal barrier in stratified squamous epithelial tissue. At the cellular level, cornification is characterised by:
production of keratin
production of small proline-rich (SPRR) proteins and transglutaminase which eventually form a cornified cell envelope beneath the plasma membrane
terminal differentiation
loss of nuclei and organelles, in the final stages of cornification
Metabolism ceases, and the cells are almost completely filled by keratin. During the process of epithelial differentiation, cells become cornified as keratin protein is incorporated into longer keratin intermediate filaments. Eventually the nucleus and cytoplasmic organelles disappear, metabolism ceases and cells undergo a programmed death as they become fully keratinized. In many other cell types, such as cells of the dermis, keratin filaments and other intermediate filaments function as part of the cytoskeleton to mechanically stabilize the cell against physical stress. It does this through connections to desmosomes, cell-cell junctional plaques, and hemidesmosomes, cell-basement membrane adhesive structures.
Cells in the epidermis contain a structural matrix of keratin, which makes this outermost layer of the skin almost waterproof, and along with collagen and elastin, gives skin its strength. Rubbing and pressure cause thickening of the outer, cornified layer of the epidermis and form protective calluses, which is useful for athletes and on the fingertips of musicians who play stringed instruments. Keratinized epidermal cells are constantly shed and replaced.
These hard, integumentary structures are formed by intercellular cementing of fibers formed from the dead, cornified cells generated by specialized beds deep within the skin. Hair grows continuously and feathers moult and regenerate. The constituent proteins may be phylogenetically homologous but differ somewhat in chemical structure and supermolecular organization. The evolutionary relationships are complex and only partially known. Multiple genes have been identified for the β-keratins in feathers, and this is probably characteristic of all keratins.
Silk[edit]
The silk fibroins produced by insects and spiders are often classified as keratins, though it is unclear whether they are phylogenetically related to vertebrate keratins.
Silk found in insect pupae, and in spider webs and egg casings, also has twisted β-pleated sheets incorporated into fibers wound into larger supermolecular aggregates. The structure of the spinnerets on spiders’ tails, and the contributions of their interior glands, provide remarkable control of fast extrusion. Spider silk is typically about 1 to 2 micrometres (µm) thick, compared with about 60 µm for human hair, and more for some mammals. The biologically and commercially useful properties of silk fibers depend on the organization of multiple adjacent protein chains into hard, crystalline regions of varying size, alternating with flexible, amorphous regions where the chains are randomly coiled.[22] A somewhat analogous situation occurs with synthetic polymers such as nylon, developed as a silk substitute. Silk from the hornet cocoon contains doublets about 10 µm across, with cores and coating, and may be arranged in up to 10 layers, also in plaques of variable shape. Adult hornets also use silk as a glue, as do spiders.
Clinical significance[edit]
Some infectious fungi, such as those that cause athlete's foot and ringworm (i.e. the dermatophytes), or Batrachochytrium dendrobatidis (Chytrid fungus), feed on keratin.[citation needed]
Diseases caused by mutations in the keratin genes include:
Epidermolysis bullosa simplex
Ichthyosis bullosa of Siemens
Epidermolytic hyperkeratosis
Steatocystoma multiplex
Keratosis pharyngis
Rhabdoid cell formation in Large cell lung carcinoma with rhabdoid phenotype[23][24]
Keratin expression is helpful in determining epithelial origin in anaplastic cancers. Tumors that express keratin include carcinomas, thymomas, sarcomas and trophoblastic neoplasms. Furthermore, the precise expression pattern of keratin subtypes allows prediction of the origin of the primary tumor when assessing metastases. For example, hepatocellular carcinomas typically express K8 and K18, and cholangiocarcinomas express K7, K8 and K18, while metastases of colorectal carcinomas express K20, but not K7.[25]
Keratin is highly resistant to digestive acids if it is ingested (Trichophagia). Because of this, cats (which groom themselves with their tongues) regularly ingest hair which will eventually result in the gradual formation of a hairball that is occasionally vomited when it becomes too big. Rapunzel syndrome is an extremely rare but potentially fatal intestinal condition in humans that is caused by Tricophagia.
See also[edit]
List of cutaneous conditions caused by mutations in keratins
List of keratins expressed in the human integumentary system
List of keratins
References[edit]
Jump up ^ OED 2nd edition, 1989 as /ˈkɛrətɪn/
Jump up ^ Entry "keratin" in Merriam-Webster Online Dictionary.
Jump up ^ Fraser, R.D.B. (1972). Keratins: Their composition, structure and biosynthesis. Bannerstone House: Charles C Thomas. pp. 3–6. ISBN 0-398-02283-6.
^ Jump up to: a b Wang, Bin (2016). "Keratin: Structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration". Progress in Materials Science. 76: 229–318. doi:10.1016/j.pmatsci.2015.06.001.
Jump up ^ "Keratin". Webster's Online Dictionary.
Jump up ^ Vincent, Julian F.V; Wegst, Ulrike G.K (July 2004). "Design and mechanical properties of insect cuticle". Arthropod Structure & Development. 33 (3): 187–199. doi:10.1016/j.asd.2004.05.006.
Jump up ^ Tombolato, Luca; Novitskaya, Ekaterina E.; Chen, Po-Yu; Sheppard, Fred A.; McKittrick, Joanna (February 2010). "Microstructure, elastic properties and deformation mechanisms of horn keratin". Acta Biomaterialia. 6 (2): 319–330. doi:10.1016/j.actbio.2009.06.033. PMID 19577667.
Jump up ^ "Keratin". Online Etymology Dictionary.
"Horn". Online Etymology Dictionary.
Jump up ^ "kerato-". Online Etymology Dictionary.
"Horn". Online Etymology Dictionary.
Jump up ^ "-in/-ine chemical suffix". Online Etymology Dictionary.
Jump up ^ Hickman, Cleveland Pendleton; Roberts, Larry S.; Larson, Allan L. (2003). Integrated principles of zoology. Dubuque, IA: McGraw-Hill. p. 538. ISBN 0-07-243940-8.
Jump up ^ Kreplak, L.; Doucet, J.; Dumas, P.; Briki, F. (July 2004). "New Aspects of the α-Helix to β-Sheet Transition in Stretched Hard α-Keratin Fibers". Biophysical Journal. 87 (1): 640–647. doi:10.1529/biophysj.103.036749. PMC 1304386  . PMID 15240497.
Jump up ^ Moll, Roland; Divo, Markus; Langbein, Lutz (2008-05-07). "The human keratins: biology and pathology". Histochemistry and Cell Biology. 129 (6): 705–733. doi:10.1007/s00418-008-0435-6. ISSN 0948-6143. PMC 2386534  .
^ Jump up to: a b Schweizer J, Bowden PE, Coulombe PA, et al. (July 2006). "New consensus nomenclature for mammalian keratins". J. Cell Biol. 174 (2): 169–74. doi:10.1083/jcb.200603161. PMC 2064177  . PMID 16831889.
Jump up ^ Hanukoglu, I.; Fuchs, E. (Nov 1982). "The cDNA sequence of a human epidermal keratin: divergence of sequence but conservation of structure among intermediate filament proteins". Cell. 31 (1): 243–52. doi:10.1016/0092-8674(82)90424-X. PMID 6186381.
^ Jump up to: a b c Hanukoglu, I.; Fuchs, E. (Jul 1983). "The cDNA sequence of a Type II cytoskeletal keratin reveals constant and variable structural domains among keratins" (PDF). Cell. 33 (3): 915–24. doi:10.1016/0092-8674(83)90034-X. PMID 6191871.
Jump up ^ Lee, CH.; Kim, MS.; Chung, BM.; Leahy, DJ.; Coulombe, PA. (Jul 2012). "Structural basis for heteromeric assembly and perinuclear organization of keratin filaments". Nat Struct Mol Biol. 19 (7): 707–15. doi:10.1038/nsmb.2330. PMC 3864793  . PMID 22705788.
Jump up ^ Voet, Donald; Voet, Judith; Pratt, Charlotte. "Proteins: Three-Dimensional Structure" (PDF). Fundamentals of Biochemistry. p. 158. Retrieved 2010-10-01. Fibrous proteins are characterized by a single type of secondary structure: a keratin is a left-handed coil of two a helices
Jump up ^ Hanukoglu I, Ezra L (Jan 2014). "Proteopedia: Coiled-coil structure of keratins". Biochem Mol Biol Educ. 42 (1): 93–94. doi:10.1002/bmb.20746. PMID 24265184.
Jump up ^ "Secondary Protein". Elmhurst.edu. Archived from the original on 2010-09-22. Retrieved 2010-09-23.
Jump up ^ "What is Keratin?". WiseGEEK. Retrieved 11 May 2014.
Jump up ^ Australia. "Spiders – Silk structure". Amonline.net.au. Archived from the original on 2009-05-08. Retrieved 2010-09-23.
Jump up ^ Shiratsuchi H, Saito T, Sakamoto A, et al. (February 2002). "Mutation analysis of human cytokeratin 8 gene in malignant rhabdoid tumor: a possible association with intracytoplasmic inclusion body formation". Mod. Pathol. 15 (2): 146–53. doi:10.1038/modpathol.3880506. PMID 11850543.
Jump up ^ Itakura E, Tamiya S, Morita K, et al. (September 2001). "Subcellular distribution of cytokeratin and vimentin in malignant rhabdoid tumor: three-dimensional imaging with confocal laser scanning microscopy and double immunofluorescence". Mod. Pathol. 14 (9): 854–61. doi:10.1038/modpathol.3880401. PMID 11557780.
Jump up ^ Omary MB, Ku NO, Strnad P, Hanada S (July 2009). "Toward unraveling the complexity of simple epithelial keratins in human disease". J. Clin. Invest. 119 (7): 1794–805. doi:10.1172/JCI37762. PMC 2701867  . PMID 19587454.
External links[edit]
Wikisource has the text of the 1920 Encyclopedia Americana article Keratin.
Composition and β-sheet structure of silk
Hair-Science.com's entry on the microscopic elements of hair
Proteopedia page on keratins
show
v
t
e
Protein: scleroproteins
Extracellular matrix
Collagen
Fibril forming
type I
COL1A1
COL1A2
type II (COL2A1)
type III
type V
COL5A1
COL5A2
COL5A3
COL24A1
COL26A1
Other
FACIT: type IX
COL9A1
COL9A2
COL9A3
type XII (COL12A1)
COL14A1
COL16A1
COL19A1
COL20A1
COL21A1
COL22A1
basement membrane: type IV
COL4A1
COL4A2
COL4A3
COL4A4
COL4A5
COL4A6
multiplexin: COL15A1
type XVIII
COL18A1
Endostatin
transmembrane: COL13A1
COL17A1
COL23A1
COL25A1
other: type VI
COL6A1
COL6A2
COL6A3
COL6A5
type VII (COL7A1)
type VIII
COL8A1
COL8A2
type X (COL10A1)
type XI
COL11A1
COL11A2
COL27A1
COL28A1
Enzymes
Prolyl hydroxylase/Lysyl hydroxylase
Cartilage associated protein/Leprecan
ADAMTS2
Procollagen peptidase
Lysyl oxidase
Laminin
alpha
LAMA1
LAMA2
LAMA3
LAMA4
LAMA5
beta
LAMB1
LAMB2
LAMB3
LAMB4
gamma
LAMC1
LAMC2
LAMC3
Other
ALCAM
Elastin
Tropoelastin
Vitronectin
FRAS1
FREM2
Decorin
FAM20C
ECM1
Matrix gla protein
Tectorin
TECTA
TECTB
Other
Keratin/Cytokeratin
Gelatin
Reticulin
Cartilage oligomeric matrix protein
show
v
t
e
Proteins of the cytoskeleton
Human
Microfilaments
and ABPs
Myofilament
Actins
A1
A2
B
C1
G1
G2
Myosins
I
MYO1A
MYO1B
MYO1C
MYO1D
MYO1E
MYO1F
MYO1G
MYO1H)
II
MYH1
MYH2
MYH3
MYH4
MYH6
MYH7
MYH7B
MYH8
MYH9
MYH10
MYH11
MYH13
MYH14
MYH15
MYH16
III
MYO3A
MYO3B
V
MYO5A
MYO5B
MYO5C
VI
MYO6
VII
MYO7A
MYO7B
IX
MYO9A
MYO9B
X
MYO10
XV
MYO15A
XVIII
MYO18A
MYO18B
LC
MYL1
MYL2
MYL3
MYL4
MYL5
MYL6
MYL6B
MYL7
MYL9
MYLIP
MYLK
MYLK2
MYLL1
Other
Tropomodulin
1
2
3
4
Troponin
T 1 2 3
C 1 2
I 1 2 3
Tropomyosin
1
2
3
4
Actinin
1
2
3
4
Arp2/3 complex
actin depolymerizing factors
Cofilin
1
2
Destrin
Gelsolin
Profilin
1
2
Titin
Other
Wiskott-Aldrich syndrome protein
Fibrillin
Filamin
FLNA
FLNB
FLNC
Espin
TRIOBP
Intermediate
filaments
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)
type I/chromosome 17
10
12
13
14
15
16
17
19
20
chromosome 12
18
none
21
type II/chromosome 12
1
2A
3
4
5
6A
6B
7
8
9
Hair keratins
(hard alpha-keratins)
type I/chromosome 17
31
32
33A
33B
34
35
36
37
38
type II/chromosome 12
81
82
83
84
85
86
Ungrouped alpha
chromosome 17
23
24
25
26
27
28
39
40
chromosome 12
71
72
73
74
75
76
77
78
79
80
Not alpha
Beta-keratin
Type 3
Desmin
GFAP
Peripherin
Vimentin
Type 4
Internexin
Nestin
Neurofilament
NEFL
NEFM
NEFH
Synemin
Syncoilin
Type 5
Nuclear lamins: A/C
B1
B2
Microtubules
and MAPs
Kinesins
KIF1A
KIF1B
KIF2A
KIF2C
KIF3B
KIF3C
KIF4A
KIF4B
KIF5A
KIF5B
KIF5C
KIF6
KIF7
KIF9
KIF11
KIF12
KIF13A
KIF13B
KIF14
KIF15
KIF16B
KIF17
KIF18A
KIF18B
KIF19
KIF20A
KIF20B
KIF21A
KIF21B
KIF22
KIF23
KIF24
KIF25
KIF26A
KIF26B
KIF27
KIFC1
KIFC2
KIFC3
Dyneins
axonemal: DNAH1
DNAH2
DNAH3
DNAH5
DNAH6
DNAH7
DNAH8
DNAH9
DNAH10
DNAH11
DNAH12
DNAH13
DNAH14
DNAH17
DNAI1
DNAI2
DNALI1
DNAL1
DNAL4
cytoplasmic: DYNC1H1
DYNC2H1
DYNC1I1
DYNC1I2
DYNC1LI1
DYNC1LI2
DYNC2LI1
DYNLL1
DYNLL2
DYNLRB1
DYNLRB2
DYNLT1
DYNLT3
Other
Tau protein
Dynactin
DCTN1
Tubulins
TUBA1A
TUBA1B
TUBA1C
TUBA3C
TUBA3D
TUBA3E
TUBA4A
TUBA8
Stathmin
Tektin
TEKT1
TEKT2
TEKT3
TEKT4
TEKT5
Dynamin
DNM1
DNM2
DNM3
Catenins
Alpha catenin
Beta catenin
APC
Plakoglobin (gamma catenin)
Delta catenin
GAN
Membrane
Dystrophin
Dystroglycan
Utrophin
Ankyrin
ANK1
ANK2
ANK3
Spectrin
SPTA1
SPTAN1
SPTB
SPTBN1
SPTBN2
SPTBN4
SPTBN5
Other
Plakins
Corneodesmosin
Desmoplakin
Dystonin
Envoplakin
MACF1
Periplakin
Plectin
Talin
TLN1
Vinculin
Plakophilin
PKP1
PKP2
Nonhuman
Major sperm proteins
Prokaryotic cytoskeleton
Crescentin
FtsZ
MreB
See also: cytoskeletal defects
Authority control
NDL: 00576167
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text:
Thermos L.L.C.
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Thermos L.L.C.
Founded
1904 in Germany
Key people
Alex Huang, PhD (CEO) [1]
Owner
Taiyo Nippon Sanso Corporation
Website
www.thermos.com
Thermos L.L.C. is the leading manufacturer worldwide of insulated food and beverage containers and other consumer products. The original company was founded in Germany in 1904.[2] In 1989, the Thermos operating companies in Japan, U.K, Canada and Australia were acquired by Nippon Sanso K.K., which had developed the world's first stainless steel vacuum bottle in 1978,[3] before it renamed itself Taiyo Nippon Sanso Corporation, as which it remains known in the present day. Taiyo Nippon Sanso also acquired the original Thermos company in Germany.[3]
Contents
[hide]
1 Thermos as a trademark
2 History
3 Connecticut
4 Expansion
5 Sales
6 Historical importance
7 References
8 External links
Thermos as a trademark[edit]
The word "thermos" is a genericized trademark used as a name for a vacuum flask.[4] From around 1910 till 1922, Thermos strove for this synonymity, as it was considered free advertising; the value of such advertising was estimated, in 1917, at between $3 and $4 million worth in American dollars alone. As the company and vacuum flask market grew, it became increasingly protective of its trademark, which it registered in 1923, following a narrow lawsuit victory over flask manufacturer W. T. Grant Company. Starting in 1935, Thermos employed a clipping service to find unauthorized usages and protested to dictionary editors who included "thermos." A 1940 internal memo said the definitions "undoubtedly would be cited against us in a lawsuit to defend the trademark. The best we can do is to try to 'purify' the definition of the word." Into the 1950s, Thermos continued its efforts to protect it, creating various products (tents, lanterns, campstoves) bearing the name to affirm it as a brand name, not an item.
In 1958, Aladdin Industries announced intent to sell "thermos bottles," and Thermos sued for infringement. In 1962, Judge Robert Anderson ruled that "thermos" was a generic term, due largely to Thermos's own publicization and lack of diligence in defending the trademark. Aladdin (or any company) could mark its bottles with a lowercase "thermos," while Thermos, then called The King-Seeley Thermos Company, retained the uppercase usage.[5]
History[edit]
Invented in 1892 by Sir James Dewar, a scientist at Oxford University, the "vacuum flask" was not manufactured for commercial use until 1904, when two German glass blowers, Reinhold Burger and Albert Aschenbrenner, formed Thermos GmbH. They held a contest to name the "vacuum flask" and a resident of Munich submitted "Thermos," which came from the Greek word therme, meaning "heat."
The thermos is commonly called the Dewar flask among chemists in recognition of its inventor, James Dewar. Dewar did not register a patent for his invention and it was subsequently patented by Thermos, to whom Dewar lost a court case in claiming the rights to the invention.[6]
Connecticut[edit]
The citizens of Norwich, Connecticut sought out the Thermos Company to build and operate a plant on the banks of the Thames River.[7] A group of citizens under the group "Norwich Boomers" rallied the community to purchase 27 acres of land for $750 an acre so that it could be used for the Thermos. The house of Dr. William H. Mason was also on the property, and it was also a part of the purchase.[7] The Italianate house was converted to be used as an office building.[8] Together, the citizens and the city raised $78,000. A contract was signed on February 14, 1912, it would make Norwich the home of the Thermos Plant and that Thermos would use Norwich's name on its advertising. Allyn L. Brown acted as attorney and provided counsel for the deal.[7] Thermos products produced in Norwich bear a stamp "Made in Norwich."[9]
The construction of the plant was a boon for Norwich, which helped the employment of the area after the decline of the textile industry.[9] The operations expanded into nearby Taftville, Connecticut and together the plants were active until they were phased out and shut down in 1988.[9][10] The Norwich site was listed as a historic district on the National Register of Historic Places in 1989.[11]
Expansion[edit]
In 1955, The American Thermos Bottle Company acquired control of Hemp and Company, Inc. of Macomb, Illinois, manufacturers of the "Little Brown Jug" and other insulated jugs and chests as well as Duncan Hines outdoor grills. To reflect the growing diversity of products, the names of the North American companies were changed in 1956. The American Thermos Bottle Company became The American Thermos Products Company, and the Canadian Thermos Bottle Co. Ltd. changed its name to Canadian Thermos Products Limited.[12]
Sales[edit]
Thermos reported revenue of $124.8 million in 1982 and $123.7 million in 1983.[13]
Historical importance[edit]
Thermos products made a major impact in the 1950s and sold over 2 million units.[citation needed] In 2004, the Smithsonian museum featured Thermos products as part of its "Taking America to Lunch" retrospective of lunch kits from the 1880s to the 1980s.[9]
References[edit]
Jump up ^ "Cool Job: Thermos CEO Alex Huang". Retrieved 1 December 2014.
Jump up ^ "About Thermos". Retrieved 30 December 2010.
^ Jump up to: a b History of the Thermos Company Kitchen Kapers
Jump up ^ 321 F.2d 577: King-Seeley Thermos Co. v. Aladdin Industries, Inc. (2d Cir. 1963)
Jump up ^ Thermos Company profile, from ReferenceForBusiness.com
Jump up ^ Frank A. J. L. James. "Dewar, James - BRITISH CHEMIST AND PHYSICIST". Advameg, Inc. Retrieved 30 December 2010.
^ Jump up to: a b c Stanley, Bill (2 April 2000). "Norwich's Fortunes Ran Hot And Cold Until The Thermos Bottle Co. Arrived". The Day. Retrieved 17 April 2014.
Jump up ^ Dale S. Plummer (1989). "National Register of Historic Places Registration: American Thermos Bottle Company Laurel Hill Plant" (PDF). National Park Service. and accompanying photos
^ Jump up to: a b c d "National Museum Honors Thermos". The Day. 14 April 2004. Retrieved 17 April 2014.
Jump up ^ "1912: Thermos". The Day. 31 December 1999. Retrieved 17 April 2014.
Jump up ^ "Weekly Register List 1989" (PDF). National Park Service. Jul 28, 1989. p. 183. Retrieved May 16, 2013.
Jump up ^ "History of the Thermos Company". Kitchen Kapers. Retrieved May 21, 2014.
Jump up ^ "Thermos Faces Competition". The Day. 28 October 1984. Retrieved 17 April 2014.
External links[edit]
Official website
Thermos Company Collection at the Thomas J. Dodd Research Center, University of Connecticut
Retrieved from "https://en.wikipedia.org/w/index.php?title=Thermos_L.L.C.&oldid=812292998"
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