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
收藏
页码：307 / 309
页数：3
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