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Protein glycosylation cellular, biotechnological, and analytical aspects by International Workshop on Protein Glycosylation (1990 Braunschweig, Germany)

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Published by VCH in Weinheim, Federal Republic of Germany, New York, NY, USA .
Written in English


  • Glycoproteins -- Synthesis -- Congresses,
  • Proteins -- Metabolism -- Congresses,
  • Glycoproteins -- Biotechnology -- Congresses,
  • Biotechnology -- congresses,
  • Glycoproteins -- analysis -- congresses,
  • Glycoproteins -- congresses,
  • Glycosylation -- congresses

Book details:

Edition Notes

Statementedited by H.S. Conradt.
SeriesGBF monographs,, v. 15
ContributionsConradt, H. S.
LC ClassificationsQP552.G59 P76 1991
The Physical Object
Paginationxii, 293 p. :
Number of Pages293
ID Numbers
Open LibraryOL1545361M
ISBN 103527283676, 1560811846
LC Control Number91024528

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Daniel C. Stein, Volker Briken, in Microbial Glycobiology, 1. Introduction. Glycosylation of proteins can substantially influence and modulate protein structure and function and appears to be involved in the fine tuning of cell–cell recognition and signalling. Until the late s, it was generally thought that protein glycosylation was restricted to eukaryotes. Protein glycosylation and glycan processing is a complex process that is poorly understood. The critical role glycoproteins play in the cell cycle along with the fact that protein glycosylation seems to become aberrant in a broad range of diseases is stimulating the need to know more about how expression and PTM of glycoproteins is regulated. Protein glycosylation is of paramount importance to the efficacy and manufacturing of therapeutic glycoproteins. Mammalian cell expression systems are the preferred method for the com-mercial production of these glycoproteins because their innate protein processing machinery, including that of protein glyco-sylation, closely resembles that in. Glycosylation is an important and highly regulated mechanism of secondary protein processing within cells. It plays a critical role in determining protein structure, function and stability. Structurally, glycosylation is known to affect the three dimensional configuration of proteins. This is of particular importance when considering protein Cited by: 8.

Protein glycosylation ultimately results in the modification of many different protein products within a given cell. Indeed, membrane and secreted proteins are nearly all glycosylated, with only rare exceptions of nonglycosylated proteins in the secretome, such as small peptide hormones, insulin, glucagon, and human serum albumin (22–24).The elaboration of complex glycans on Cited by: Proteins Biochemistry and Biotechnology 2e is a definitive source of information for all those interested in protein science, and particularly the commercial production and isolation of specific proteins, and their subsequent utilization for applied purposes in industry and medicine. Fully updated throughout with new or fundamentally revised sections on proteomics as, . Glycosylation, the attachment of sugar moieties to proteins, is a post-translational modification (PTM) that provides greater proteomic diversity than other PTMs. Glycosylation is critical for a wide range of biological processes, including cell attachment to the extracellular matrix and protein–ligand interactions in the cell. O-glycosylation occurring outside mucin regions is difficult to predict accurately and so is usually only detected after production of a protein. As O-glycosylation occurs in the Golgi, it has little bearing on the early stages of protein folding and therefore sites found to be O-glycosylated can be engineered out of the protein by site Cited by: 4.

The major sites of protein glycosylation in the body are ER, Golgi body, nucleus and the cell fluid. Protein glycosylation can be categorized in two main types: a) N-linked glycosylation: It begins with the addition of a sugar precursor to an asparagine amino acid. It contains glucose, mannose and n-acetylglucosamine molecules. Glycosylation is an important modification to eukaryotic proteins because the added sugar residues are often used as molecular flags or recognition signals to other cells than come in contact with them. There are two types of protein glycosylation, both of which require import of the target polypeptide into the ER. Glycosylation refers to the covalent bonding of blood glucose to the red blood cells. Normally, only a small percentage of blood glucose, usually between %- 6%, is covalently linked to the red blood cells in hemoglobin of the non diabetes population. This value is commonly referred to as glycosylated hemoglobin or more specifically. There are two basic types of protein glycosylation: N-glycosylation and O-glycosylation. These have significant differences in terms of their biosynthesis and structure, as well as location within the protein chain. N-glycans are pro-duced from a mer precursor structure that is added to Asparagine residues in the consensus sequence Asn-X-Ser.