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V. G. Vaze College of Arts, Science and Commerce
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V. G. Vaze College of Arts, Science & Commerce (Kelkar College)
Address
V. G. Vaze College of Arts, Science & Commerce (Kelkar College)
Location in Mumbai
Mithagar Road
Courses[edit source]
Bhausaheb Kelkar was an industrialist who manufactured fragrances. He had been promoting educational activities through donations to institutions and grants to underprivileged students. A Kelkar Education Trust was set up by Bhausaheb in Mulund in 1979 to start a college.[1] Kelkar College was started by the Kelkar-Vaze family in the year 1984. The college managed to get affiliation from University of Mumbai soon and is the youngest college to get permanent affiliation from the university of Mumbai.
The college offers various professional courses, Post graduate programs, and advanced diploma under the dual degree program. PhD: Economics, Zoology, Chemistry, Botany, Life sciences PG Programmes: PG by research in Botany, Zoology, Chemistry PG by papers in Zoology, Chemistry, MSc IT, MSc Biotech UG Degree: Commerce, Arts and Science. In all 122 subject combinations.
Self-financing Collaborative programme: Post Graduate Diploma in Perfumery and Cosmetic Management
Mulund, Maharashtra, 400081
India
Coordinates
19°09′47″N 72°57′27″E / 19.162990°N 72.957544°E / 19.162990; 72.957544Coordinates: 19°09′47″N 72°57′27″E / 19.162990°N 72.957544°E / 19.162990; 72.957544
Information
Type
Private
Established
1984
Founder
Shri Govind Damdodar alias Bhausaheb Kelkar
Principal
Dr. B. B. Sharma
Medium of language
English
Campus type
Urban
Affiliation
University of Mumbai
Website
VazeCollge.net
Vinayak Ganesh Vaze College of Arts, Science & Commerce (more commonly known as Kelkar College), a Mumbai University affiliated college located in Mulund East, Mumbai. The Kelkar Education Trust, in memory of its founder trustee, late Shri Annasaheb Vaze, established Vinayak Ganesh Vaze College of Arts, Science & Commerce in 1984.
Contents
1 History
2 Location
3 Affiliation and accreditation
4 Courses
5 Students' Council
6 Festival
7 Famous alumni
8 See also
9 References
10 External links
History[edit]
Bhausaheb Kelkar was an industrialist who manufactured fragrances. He had been promoting educational activities through donations to institutions and grants to underprivileged students. A Kelkar Education Trust was set up by Bhausaheb in Mulund in 1979 to start a college.[1] Kelkar College was started by the Kelkar-Vaze family in the year 1984. The college managed to get affiliation from University of Mumbai soon and is the youngest college to get permanent affiliation from the university of Mumbai.[2]
Location[edit]
It is located at Mithagar area of Mulund East, a northeastern suburb of Mumbai.
Affiliation and accreditation[edit]
The College is permanently affiliated to the University of Mumbai since 1990. It was also later recognized by UGC(University grants commission).[3] Kelkar College is the first affiliated Arts, Science and Commerce institution in the state of Maharashtra which was assessed for accreditation by National Assessment and Accreditation Council(NAAC), which the institution of UGC had started. College received five star status in 1998, reassessed in 2005 and assessed for third cycle in 2012 (Third time) with an "A" grade from NAAC.[4]
Courses[edit]
The college offers various professional courses, Post graduate programs, and advanced diploma under the dual degree program.
PhD: Economics, Zoology, Chemistry, Botany, Life sciences
PG Programmes: PG by research in Botany, Zoology, Chemistry
PG by papers in Zoology, Chemistry, MSc IT, MSc Biotech
UG Degree: Commerce, Arts and Science. In all 122 subject combinations.
Self-financing Collaborative programme: Post Graduate Diploma in Perfumery and Cosmetic Management[5][6]
Students' Council[edit]
As per section 40 (2)(b) of Maharashtra University Act, 1994,[7] the College has set up a body of 22 nominated students, on behalf of all the students of the college, to represent various classes and disciplines.
Festival[edit]
The college hosts an inter college festival named "Dimensions".[8] It generally takes place during the month of December/January every year. Every year a theme is chosen, and accordingly the fest revolves around it.
Year
Theme Name
2013 Back to Innocence [9]
2014 Tour De World [10]
2015 The Age of Superheroes [11]
2016 The Theatre Of Dreams 2017 Cosmic Udaan.
Famous alumni[edit]
This article needs additional citations for verification. Please help improve this article by adding citations to reliable sources. Unsourced material may be challenged and removed. (October 2015) (Learn how and when to remove this template message)
Rucha Hasabnis, Hindi Television Actress[citation needed]
Yukta Mookhey, Miss World 1999[12]
Tejashree Pradhan, Marathi Television Actress[citation needed]
Manasi Salvi, Hindi Television Actress[citation needed]
Ajinkya Rahane, Indian Cricketer [13] [14]
Hemant Lagvankar, Science communicator and educational consultant, Recipient of the National Award of Government of India, New Delhi in 2014
Prajakta Koli, Youtuber and Blogger[citation needed]
See also[edit]
University of Mumbai
References[edit]
Jump up ^ "Kelkar Trust's Vaze College blends sports with studies - Hindustan Times". www.hindustantimes.com/. Retrieved 30 October 2015.
Jump up ^ "Welcome to V.G.Vaze College". Vazecollege.net. Retrieved 20 September 2014.
Jump up ^ "Welcome to V.G.Vaze College". Vazecollege.net. Retrieved 20 September 2014.
Jump up ^ "Welcome to V.G.Vaze College". Vazecollege.net. Retrieved 20 September 2014.
Jump up ^ "Welcome to V.G.Vaze College". Vazecollege.net. Retrieved 20 September 2014.
Jump up ^ "Vaze College Mumbai Cosmetology Centre". www.favors101.info. Retrieved 3 March 2015.
Jump up ^ The Maharashtra Universities Act, 1994 (PDF). pp. 51–53. Retrieved 23 September 2014.
Jump up ^ "Dimensions - Kelkar College Fest". vazecollege.net. Retrieved 6 October 2014.
Jump up ^ "Dimensions 2013-14". festpav.com. Retrieved 5 October 2015.
Jump up ^ "Official Theme for Dimensions 2015". Dimensions 2014-15 - facebook.com. Retrieved 5 October 2015.
Jump up ^ "Official Theme for Dimensions 2015". Dimensions - The Fest. - facebook.com. Retrieved 5 October 2015.
Jump up ^ Nair, Sandhya (19 June 2004). "The definitive guide to Mumbai colleges". Mid Day. Retrieved 30 October 2015.
Jump up ^ https://www.instagram.com/p/BB0LT-VlCMe/?taken-by=radhika_dhopavkar&hl=en
Jump up ^ http://m.indiatvnews.com/sports/cricket/know-radhika-better-half-of-ajinkya-rahane-new-indian-captain-17664.html/page/4
External links[edit]
Kelkar College Official website
Prospectus of College
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Glycoprotein
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Not to be confused with peptidoglycan, proteoglycan, or glycopeptide.
N-linked protein glycosylation (N-glycosylation of N-glycans) at Asn residues (Asn-x-Ser/Thr motifs) in glycoproteins.[1]
Glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to polypeptide side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated.
In proteins that have segments extending extracellularly, the extracellular segments are also often glycosylated. Glycoproteins are also often important integral membrane proteins, where they play a role in cell–cell interactions. It is important[according to whom?] to distinguish endoplasmic reticulum-based glycosylation of the secretory system without reversible cytosolic-nuclear glycosylation. Glycoprotein of the cytosol and nucleus can be modified through the reversible addition of a single GlcNAc residue that is considered reciprocal to phosphorylation and the functions of these are likely to be additional regulatory mechanism that controls phosphorylation-based signalling.[2] In contrast, classical secretory glycosylation can be structurally essential. For example, inhibition of asparagine-linked, i.e. N-linked, glycosylation can prevent glycoprotein folding and full inhibition can be toxic to an individual cell. In contrast, perturbation of terminal processing, which occurs in the Golgi apparatus, is dispensable for isolated cells (as evidence by survival with glycosides inhibitors) but can lead to human disease (congenital disorders of glycosylation) and can be lethal in animal models. It is therefore likely that the fine processing of glycans is important for endogeneous functionality, such as cell trafficking, but that this is likely to have been secondary to its role in host-pathogen interactions. A famous example of this latter effect is the ABO blood system.[citation needed]
Contents
[hide]
1 Types of glycosylation
2 Monosaccharides
3 Examples
4 Hormones
5 Functions
6 Analysis
7 See also
8 Notes and references
9 External links
Types of glycosylation[edit]
There are several types of glycosylation, although the first two are the most common.
In N-glycosylation, sugars are attached to nitrogen, typically on the amide side-chain of asparagine.
In O-glycosylation, sugars are attached to oxygen, typically on serine or threonine but also on non-canonical amino acids such as hydroxylysine & hydroxyproline.
In P-glycosylation, sugars are attached to phosphorus on a phosphoserine.
In C-glycosylation, sugars are attached directly to carbon, such as in the addition of mannose to tryptophan.
In glypiation, a GPI glycolipid is attached to the C-terminus of a polypeptide, serving as a membrane anchor.
Monosaccharides[edit]
Eight sugars commonly found in glycoproteins.
Monosaccharides commonly found in eukaryotic glycoproteins include:[3]:526
The principal sugars found in human glycoproteins[4]
Sugar
Type
Abbreviation
β-D-Glucose Hexose Glc
β-D-Galactose Hexose Gal
β-D-Mannose Hexose Man
α-L-Fucose Deoxyhexose Fuc
N-Acetylgalactosamine Aminohexose GalNAc
N-Acetylglucosamine Aminohexose GlcNAc
N-Acetylneuraminic acid Aminononulosonic acid
(Sialic acid) NeuNAc
Xylose Pentose Xyl
The sugar group(s) can assist in protein folding or improve proteins' stability.
Examples[edit]
One example of glycoproteins found in the body is mucins, which are secreted in the mucus of the respiratory and digestive tracts. The sugars when attached to mucins give them considerable water-holding capacity and also make them resistant to proteolysis by digestive enzymes.
Glycoproteins are important for white blood cell recognition, especially in mammals.[citation needed] Examples of glycoproteins in the immune system are:
molecules such as antibodies (immunoglobulins), which interact directly with antigens.
molecules of the major histocompatibility complex (or MHC), which are expressed on the surface of cells and interact with T cells as part of the adaptive immune response.
sialyl Lewis X antigen on the surface of leukocytes.
H antigen of the ABO blood compatibility antigens. Other examples of glycoproteins include:
gonadotropins (luteinizing hormone a follicle-stimulating hormone)
glycoprotein IIb/IIIa, an integrin found on platelets that is required for normal platelet aggregation and adherence to the endothelium.
components of the zona pellucida, which surrounds the oocyte, and is important for sperm-egg interaction.
structural glycoproteins, which occur in connective tissue. These help bind together the fibers, cells, and ground substance of connective tissue. They may also help components of the tissue bind to inorganic substances, such as calcium in bone.
Glycoprotein-41 (gp41) and glycoprotein-120 (gp120) are HIV viral coat proteins.
Soluble glycoproteins often show a high viscosity, for example, in egg white and blood plasma.
Miraculin, is a glycoprotein extracted from Synsepalum dulcificum a berry which alters human tongue receptors to recognize sour foods as sweet.[5]
Variable surface glycoproteins allow the sleeping sickness Trypanosoma parasite to escape the immune response of the host.
The viral spike of the human immunodeficiency virus is heavily glycosylated.[6] Approximately half the mass of the spike is glycosylation and the glycans act to limit antibody recognition as the glycans are assembled by the host cell and so are largely 'self'. Over time, some patients can evolve antibodies to recognise the HIV glycans and almost all so-called 'broadly neutralising antibodies (bnAbs) recognise some glycans. This is possible mainly because the unusually high density of glycans hinders normal glycan maturation and they are therefore trapped in the premature, high-mannose, state.[7][8] This provides a window for immune recognition. In addition, as these glycans are much less variable than the underlying protein, they have emerged as promising targets for vaccine design.[9]
Hormones[edit]
Hormones that are glycoproteins include:
Follicle-stimulating hormone
Luteinizing hormone
Thyroid-stimulating hormone
Human chorionic gonadotropin
Alpha-fetoprotein
Erythropoietin (EPO)
Functions[edit]
Some functions served by glycoproteins[3]:524
Function
Glycoproteins
Structural molecule Collagens
Lubricant and protective agent Mucins
Transport molecule Transferrin, ceruloplasmin
Immunologic molecule Immunoglobulins,[10] histocompatibility antigens
Hormone Human chorionic gonadotropin (HCG), thyroid-stimulating hormone (TSH)
Enzyme Various, e.g., alkaline phosphatase, patatin
Cell attachment-recognition site Various proteins involved in cell–cell (e.g., sperm–oocyte), virus–cell, bacterium–cell, and hormone–cell interactions
Antifreeze protein Certain plasma proteins of coldwater fish
Interact with specific carbohydrates Lectins, selectins (cell adhesion lectins), antibodies
Receptor Various proteins involved in hormone and drug action
Affect folding of certain proteins Calnexin, calreticulin
Regulation of development Notch and its analogs, key proteins in development
Hemostasis (and thrombosis) Specific glycoproteins on the surface membranes of platelets
Analysis[edit]
A variety of methods used in detection, purification, and structural analysis of glycoproteins are[3]:525[10][11]

Some important methods used to study glycoproteins
Method
Use
Periodic acid-Schiff stain Detects glycoproteins as pink bands after electrophoretic separation.
Incubation of cultured cells with glycoproteins as radioactive decay bands Leads to detection of a radioactive sugar after electrophoretic separation.
Treatment with appropriate endo- or exoglycosidase or phospholipases Resultant shifts in electrophoretic migration help distinguish among proteins with N-glycan, O-glycan, or GPI linkages and also between high mannose and complex N-glycans.
Agarose-lectin column chromatography, lectin affinity chromatography To purify glycoproteins or glycopeptides that bind the particular lectin used.
Lectin affinity electrophoresis Resultant shifts in electrophoretic migration help distinguish and characterize glycoforms, i.e. variants of a glycoprotein differing in carbohydrate.
Compositional analysis following acid hydrolysis Identifies sugars that the glycoprotein contains and their stoichiometry.
Mass spectrometry Provides information on molecular mass, composition, sequence, and sometimes branching of a glycan chain. It can also be used for site-specific glycosylation profiling.[10]
NMR spectroscopy To identify specific sugars, their sequence, linkages, and the anomeric nature of glycosidic chain.
Multi-angle light scattering In conjunction with size-exclusion chromatography, UV/Vis absorption and differential refractometry, provides information on molecular mass, protein-carbohydrate ratio, aggregation state, size, and sometimes branching of a glycan chain. In conjunction with composition-gradient analysis, analyzes self- and hetero-association to determine binding affinity and stoichiometry with proteins or carbohydrates in solution without labeling.
Dual Polarisation Interferometry Measures the mechanisms underlying the biomolecular interactions, including reaction rates, affinities and associated conformational changes.
Methylation (linkage) analysis To determine linkage between sugars.
Amino acid or cDNA sequencing Determination of amino acid sequence.
See also[edit]
Ero1
Female sperm storage
Glycocalyx
Glycome
Glycopeptide
Gp120
Gp41
Miraculin
P-glycoprotein
Proteoglycan
Ribophorin
Notes and references[edit]
Jump up ^ Ruddock & Molinari (2006) Journal of Cell Science 119, 4373–4380
Jump up ^ Funakoshi Y, Suzuki T (January 2009). "Glycobiology in the cytosol: The bitter side of a sweet world". Biochim. Biophys. Acta. 1790 (2): 81–94. doi:10.1016/j.bbagen.2008.09.009. PMID 18952151.
^ Jump up to: a b c Robert K. Murray, Daryl K. Granner & Victor W. Rodwell: "Harper's Illustrated Biochemistry 27th Ed.", McGraw–Hill, 2006
Jump up ^ Glycan classification SIGMA
Jump up ^ Theerasilp S, Kurihara Y (August 1988). "Complete purification and characterization of the taste-modifying protein, miraculin, from miracle fruit". J. Biol. Chem. 263 (23): 11536–9. PMID 3403544.
Jump up ^ Pritchard, Laura K.; Vasiljevic, Snezana; Ozorowski, Gabriel; Seabright, Gemma E.; Cupo, Albert; Ringe, Rajesh; Kim, Helen J.; Sanders, Rogier W.; Doores, Katie J. (2015-06-16). "Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers". Cell Reports. 11 (10): 1604–1613. doi:10.1016/j.celrep.2015.05.017. ISSN 2211-1247. PMC 4555872  . PMID 26051934.
Jump up ^ Pritchard, Laura K.; Spencer, Daniel I. R.; Royle, Louise; Bonomelli, Camille; Seabright, Gemma E.; Behrens, Anna-Janina; Kulp, Daniel W.; Menis, Sergey; Krumm, Stefanie A. (2015-06-24). "Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies". Nature Communications. 6: 7479. Bibcode:2015NatCo...6E7479P. doi:10.1038/ncomms8479. PMC 4500839  . PMID 26105115.
Jump up ^ Behrens, Anna-Janina; Vasiljevic, Snezana; Pritchard, Laura K.; Harvey, David J.; Andev, Rajinder S.; Krumm, Stefanie A.; Struwe, Weston B.; Cupo, Albert; Kumar, Abhinav (2016-03-10). "Composition and Antigenic Effects of Individual Glycan Sites of a Trimeric HIV-1 Envelope Glycoprotein". Cell Reports. 14 (11): 2695–2706. doi:10.1016/j.celrep.2016.02.058. ISSN 2211-1247. PMC 4805854  . PMID 26972002.
Jump up ^ Crispin, Max; Doores, Katie J (2015-04-01). "Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design". Current Opinion in Virology. Viral pathogenesis • Preventive and therapeutic vaccines. 11: 63–69. doi:10.1016/j.coviro.2015.02.002. PMC 4827424  . PMID 25747313.
^ Jump up to: a b c Maverakis E, Kim K, Shimoda M, Gershwin M, Patel F, Wilken R, Raychaudhuri S, Ruhaak LR, Lebrilla CB (2015). "Glycans in the immune system and The Altered Glycan Theory of Autoimmunity". J Autoimmun. 57 (6): 1–13. doi:10.1016/j.jaut.2014.12.002. PMC 4340844  . PMID 25578468.
Jump up ^ Dell A (2001). "Glycoprotein Structure Determination by Mass Spectrometry". Science. 291 (5512): 2351–2356. doi:10.1126/science.1058890. ISSN 0036-8075.
External links[edit]
Glycan Recognizing Proteins
Structure of Glycoprotein and Carbohydrate Chain – Home Page for Learning Environmental Chemistry
Biochemistry 5thE 11.3. Carbohydrates Can Be Attached to Proteins to Form Glycoproteins
Carbohydrate Chemistry and Glycobiology: A Web Tour SPECIAL WeB SUPPLEMENT Science 23 March 2001 Vol 291, Issue 5512, Pages 2263–2502
Glycoproteins at the US National Library of Medicine Medical Subject Headings (MeSH)
Emanual Maverakis et. al. "Glycans in the immune system and The Altered Glycan Theory of Autoimmunity" (PDF).
Biological Importance of the glycosylation of a protein
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