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- W2487667075 abstract "Publisher Summary This chapter elaborates the structural chemistry and the biological aspects of O-sialoglycoprotein endopeptidase. The enzyme O-sialoglycoprotein endopeptidase, abbreviated as glycoprotease, derives its name from its unique specificity for the proteolytic cleavage of glycoproteins, and all known substrates are glycoproteins rich in anionic sialoglycans and or sulfoglycans O-linked to threonine or serine residues. Human glycophorin A, either in situ in erythrocyte ghost membrane or free in solution, is cleaved by the enzyme at several peptide bonds, principally Arg31–Asp32, but extensive degradation occurs at other sites and the peptide bond specificity is apparently broad. The cleavage of glycophorin A is most extensive within the heavily glycosylated extracellular domain, which bears 15 O-linked glycans and one N-linked glycan. Other cell surface O-sialoglycoproteins that are cleaved by the glycoprotease include the human hematopoietic stem cell antigen CD34; leukosialin CD43; hyaluronate receptor CD44; leukocyte common antigen CD45; ligands for L-selectin and P-selectin; receptor for interleukin 7; human tumor cell antigen epitectin; human platelet glycoprotein Ib(a); cranin, which is a laminin-binding membrane O-sialoglycoprotein; human vascular adhesion protein VAP-1; and Epstein–Barr viral glycoproteins gpl50 and gp350." @default.
- W2487667075 created "2016-08-23" @default.
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- W2487667075 date "2004-01-01" @default.
- W2487667075 modified "2023-09-25" @default.
- W2487667075 title "O-Sialoglycoprotein endopeptidase" @default.
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- W2487667075 doi "https://doi.org/10.1016/b978-0-12-079611-3.50304-9" @default.
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