RELAXATION STUDIES OF ENZYMES - RAPID ISOMERIZATION IN DEOXYRIBONUCLEASE-I

被引：2

作者：

FELTCH, SM ^{[1
]}

STUEHR, JE ^{[1
]}

机构：

[1] CASE WESTERN RESERVE UNIV, DEPT CHEM, CLEVELAND, OH 44106 USA

来源：

BIOCHEMISTRY | 1979年 / 18卷 / 10期

关键词：

D O I：

10.1021/bi00577a024

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：

Temperature-jump relaxation studies in deoxyribonuclease I were carried out at 10 °C and [I] =0.1 M. The single observed relaxation time, which varied from l0-4 to 10-5 s, was characterized as a function of enzyme concentration, pH, and indicator concentration. The concentration and pH dependences of the relaxation time are in quantitative agreement with a mechanism involving an isomerization of the enzyme coupled to a rapid proton ionization process. The best fit forward and reverse isomerization rate constants are 6.5?103 and 7.2?104 s-1, respectively; the apparent pK is 5.7. The addition of urea brought about reductions in both the amplitude of the relaxation effect and the enzyme activity. © 1979, American Chemical Society. All rights reserved.

引用

页码：2000 / 2004

页数：5

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