DETECTION OF A GLYCOSYLATED FORM OF HEN EGG-WHITE LYSOZYME

被引：8

作者：

TRUDEL, J ^{[1
]}

ASSELIN, A ^{[1
]}

机构：

[1] UNIV LAVAL,FAC SCI AGR & ALIMENTAT,DEPT PHYTOL,ST FOY,PQ G1K 7P4,CANADA

来源：

BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE | 1995年 / 73卷 / 5-6期

关键词：

LYSOZYME; GLYCOSYLATION; SEQUENTIAL PAGE; N-TERMINUS MICROSEQUENCING;

D O I：

10.1139/o95-038

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：

By assaying lysozyme activity after denaturing polyacrylamide gel electrophoresis of commercial hen egg white lysozyme preparations, minor lysozymal activity was detected as an 18-kDa protein. After electrophoretic purification for microsequencing, the N-terminus sequence of the 18-kDa lysozyme was found to be identical with mature 14.4-kDa hen egg white lysozyme. The 18-kDa hen egg white lysozyme was judged to be glycosylated based on a 3.6-kDa decrease in molecular mass after N-glycosidase F treatment, binding to concanavalin A - Sepharose, and staining with periodate - Schiff's reagent. The minor form corresponded to about 0.3% of lyzozyme molecules.

引用

页码：307 / 309

页数：3

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