RELATIONSHIPS BETWEEN STABILITY OF THREONINE DEAMINASE AND ITS APPARENT KINETICS

被引：16

作者：

HARDING, WM

机构：

[1] Department of Chemistry, Sam Houston State College, Huntsville, TX

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1969年 / 129卷 / 01期

关键词：

D O I：

10.1016/0003-9861(69)90149-0

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：

If precautions are taken to stabilize biosynthetic threonine deaminase of Escherichia coli during the assay, the enzyme exhibits normal Michaelis-Menten kinetics. Loss of activity during 10 min at 27 ° is almost complete when the diluted enzyme is in the presence of low concentrations of threonine and potassium phosphate buffer (pH 8.2). An increase in stability is effected by an increase in the concentration of either the enzyme preparation, threonine, or buffer. © 1969.

引用

页码：57 / &

共 17 条

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