PURIFICATION AND PROPERTIES OF BETA-N-ACETYLHEXOSAMINIDASE-A FROM PIG BRAIN

被引:5
作者
GARCIAALONSO, J [1 ]
REGLERO, A [1 ]
CABEZAS, JA [1 ]
机构
[1] UNIV SALAMANCA,FAC BIOL,DEPT BIOCHEM & MOLEC BIOL,SALAMANCA,SPAIN
来源
INTERNATIONAL JOURNAL OF BIOCHEMISTRY | 1990年 / 22卷 / 06期
关键词
D O I
10.1016/0020-711X(90)90043-3
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
1. 1. Adult pig brain β-N-acetylhexosaminidase was separated into four different forms by ion exchange chromatography on diethylaminoethyl-cellulose. 2. 2. Form A was purified 1300-1500 fold by an unusual procedure, the technique of ampholyte displacement, followed by chromatography on concanavalin A Sepharose. 3. 3. The enzyme catalyses the hydrolysis of both β-N-acetylglucosaminides and β-N-acetylgalactosaminides. 4. 4. The kinetic studies support the evidence of the association of both activities to a single protein, and at the same active site. 5. 5. A natural substrate, N,N′-diacetylchitobiose, is also hydrolyzed, but not ovalbumin. 6. 6. This enzyme may be considered as an exoglycosidase. © 1990.
引用
收藏
页码:645 / 651
页数:7
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