STEADY-STATE KINETIC STUDY OF ACTION OF RIBONUCLEASE-A, INVOLVING A CONFORMATIONAL CHANGE BETWEEN 30-DEGREES-C AND 40-DEGREES-C

被引：23

作者：

MATHESON, RR ^{[1
]}

SCHERAGA, HA ^{[1
]}

机构：

[1] CORNELL UNIV,BAKER LAB,ITHACA,NY 14853

来源：

BIOCHEMISTRY | 1979年 / 18卷 / 12期

关键词：

D O I：

10.1021/bi00579a002

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：

The steady-state kinetics of the reaction of ribonuclease A with cyclic cytidine 2‘,3‘-phosphate as substrate are investigated as a function of temperature at pH 5 and ionic strength 0.1 M. The results suggest, but cannot prove, that a conformational change near 32 °C is involved in the rate-limiting step of the reaction mechanism. This conformational change is proposed to be the same one that was observed in studies of the free enzyme and of enzyme-inhibitor complexes near the same temperature. © 1979, American Chemical Society. All rights reserved.

引用

页码：2446 / 2450

页数：5

共 48 条

[31] NUCLEAR MAGNETIC RESONANCE STUDIES OF STRUCTURE AND BINDING SITES OF ENZYMES .8. INHIBITOR BINDING TO RIBONUCLEASE [J].