Isolation of a glycosylated form of the chicken eggshell protein ovocleidin and determination of the glycosylation site.: Alternative glycosylation/phosphorylation at an N-glycosylation sequon

被引:44
作者
Mann, K [1 ]
机构
[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany
关键词
ovocleidin; eggshell; glycosylation; phosphorylation;
D O I
10.1016/S0014-5793(99)01586-0
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
Ovocleidin, a major protein of the avian eggshell calcified layer, occurs in the eggshell soluble organic matrix in at least two forms. The major form is a phosphoprotein with two phosphorylated serines (OC-17) which was sequenced recently. A minor form is a glycosylated protein with identical sequence and only one phosphorylated serine (OC-23), The site of glycosylation is Asn(59), the only asparagine in the amino acid sequence contained in the N-glycosylation site consensus sequence, N-A-S. Ser(61), which is part of this site, is phosphorylated in OC-17 but not in OC-23 indicating that the two modifications are mutually exclusive, This is the first example of alternative glycosylation/phosphorylation occurring at an N-glycosylation site. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:12 / 14
页数:3
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