HUMAN ACID BETA-GLUCOSIDASE - GLYCOSYLATION IS REQUIRED FOR CATALYTIC ACTIVITY

被引:40
作者
GRACE, ME
GRABOWSKI, GA
机构
[1] Division of Medical and Molecular Genetics, Department of Pediatrics, Mount Sinai School of Medicine, New York, NY 10029, One Gustave Levy Place
关键词
D O I
10.1016/0006-291X(90)92388-G
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
The role of oligosaccharide modification in human acid β-glucosidase function was investigated. This lysosomal enzyme has five putative N-glycosylation sites, four of which are occupied. The unglycosylated human protein was stable when expressed in bacteria or in Spodoptera frugiperda cells in the presence of tunicamycin but lacked catalytic activity. Deglycosylation of purified acid β-glucosidase from human placenta with N-Glycanase™ under native conditions resulted in the removal of an accessible oligosaccharide chain from a single site with no effect on activity, whereas studies demonstrate that occupancy of at least one glycosylation site is required for the formation and maintenance of acid β-glucosidase in an active conformation. © 1990.
引用
收藏
页码:771 / 777
页数:7
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