CHARACTERIZATION OF O-LINKED GLYCOSYLATION MOTIFS IN THE GLYCOPEPTIDE DOMAIN OF BOVINE KAPPA-CASEIN

被引:77
|
作者
PISANO, A
PACKER, NH
REDMOND, JW
WILLIAMS, KL
GOOLEY, AA
机构
[1] MACQUARIE UNIV, SCH BIOL SCI, SYDNEY, NSW 2109, AUSTRALIA
[2] MACQUARIE UNIV, CTR ANALYT BIOTECHNOL, SYDNEY, NSW 2109, AUSTRALIA
基金
英国医学研究理事会;
关键词
KAPPA-CASEIN; O-GLYCOSYLATION MOTIF; SOLID-PHASE EDMAN DEGRADATION;
D O I
10.1093/glycob/4.6.837
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
kappa-Casein is the major glycoprotein in bovine milk, It has a proteinase-sensitive (chymosin) site which cleaves the glycoprotein into two segments: N-terminal-para-kappa-casein domain and the C-terminal kappa-casein macroglycopeptide domain which is highly heterogeneous in oligosaccharide content, We have identified six sites of O-glycosylation on the macroglycopeptide by solid-phase Edman degradation: Thr121, Thr131, Thr133, Thr136 (A variant only), Thr142 and Thr165. No Ser residues are glycosylated, The glycosylation status of 15 of 17 potential O-glycosylation sites in the B variant was accurately predicted using the four peptide moths previously proposed for the glycosylation of human glycophorin A (Pisano, A., Redmond, J. W., Williams, K. L. and Gooley, A. A., Glycobiology, 3, 429-435, 1993), provided one additional assumption is made concerning an inhibitory role for a nearby Ile.
引用
收藏
页码:837 / 844
页数:8
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