ISOLATION AND PURIFICATION OF AMYLOGLUCOSIDASE FROM HALOBACTERIUM-SODOMENSE

被引:16
作者
CHAGA, G [1 ]
PORATH, J [1 ]
ILLENI, T [1 ]
机构
[1] UNIV UPPSALA,BMC,PILOT PLANT,S-75123 UPPSALA,SWEDEN
关键词
D O I
10.1002/bmc.1130070504
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Amyloglucosidase from Halobacterium sodomense was purified by a combination of hydrophobic interaction chromatography and immobilized metal ion affinity chromatography at analytical and preparative scale with 75% recovery. The enzyme was found to be a dimer of two different subunits with molecular weights of 72,000 and 82,000 D, respectively, combining in a 175,000 D native protein. The specific activity, K(M), and amino acid composition of the enzyme was determined.
引用
收藏
页码:256 / 261
页数:6
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