BINDING OF SPIN-LABELED DERIVATIVES OF NAD+ AND ITS STRUCTURAL COMPONENTS TO PIG SKELETAL-MUSCLE LACTATE-DEHYDROGENASE

被引：4

作者：

DEPARADE, MP

TROMMER, WE

机构：

[1] UNIV STUTTGART,INST BIOCHEM,D-7000 STUTTGART 80,FED REP GER

[2] UNIV STUTTGART,INST ORGAN CHEM,D-7000 STUTTGART 80,FED REP GER

[3] UNIV STUTTGART,INST ISOTOPENFORSCH,D-7000 STUTTGART 80,FED REP GER

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 568卷 / 01期

关键词：

(Pig skeletal muscle); Coenzyme binding; Cooperativity; Lactate dehydrogenase; NAD[!sup]+[!/sup; Spin-label;

D O I：

10.1016/0005-2744(79)90284-5

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 binding of spin-labeled derivatives of NAD+ and its structural components to pig skeletal muscle lactate dehydrogenase (l-lactate:NAD+ oxidoreductase, EC 1.1.1.27) is described. In contrast to results previously obtained with the heart muscle isozyme (Wenzel, H.R., Pfleiderer, G., Trommer, W.E., Paschenda, K. and Redhardt, A. (1976) Biochim. Biophys. Acta 452, 292-301), no significant increase is observed in the binding constant of N6, SL-ADP as compared N6-SL-AMP. This different behavior can be explained by the substitution of glutamine-31 for alanine in the muscle isozyme, which has been proposed to account for the tighter binding of NADH to the heart type. In both isozymes the binding of the spin-labled coenzyme itself is weaker than found for its structural components. © 1979.

引用

页码：177 / 182

页数：6

共 23 条

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