Crystallization of β-galactosidase does not reduce the range of activity of individual molecules

被引：32

作者：

Shoemaker, GK

Juers, DH

Coombs, JML

Matthews, BW

Craig, DB ^{[1
]}

机构：

[1] Univ Winnipeg, Dept Chem, Winnipeg, MB R3B 2E9, Canada

[2] Univ Oregon, Inst Mol Biol, Eugene, OR 97405 USA

[3] Univ Oregon, Howard Hughes Med Inst, Eugene, OR 97405 USA

来源：

BIOCHEMISTRY | 2003年 / 42卷 / 06期

关键词：

D O I：

10.1021/bi0204138

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 use of a capillary electrophoresis-based procedure, it is possible to measure the activity of individual molecules of beta-galactosidase. Molecules from the crystallized enzyme as well as the original enzyme preparation used to grow the crystals both displayed a range of activity of 20-fold or greater. beta-Galactosidase molecules obtained from two different crystals had indistinguishable activity distributions of 31 600 +/- 1100 and 31 800 +/- 1100 reactions min(-1) (enzyme molecule)(-1). This activity was found to be significantly different from that of the enzyme used to grow the crystals, which showed an activity distribution of 38 500 +/- 900 reactions min(-1) (enzyme molecule)(-1).

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页码：1707 / 1710

页数：4

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