烟酰胺腺嘌呤二核苷酸（NAD+）及其结构成分的自旋标记衍生物与猪骨骼肌乳酸脱氢酶的结合
The binding of spin-labeled derivatives of NAD+ and its structural components to pig skeletal muscle lactate dehydrogenase.
作者信息
Deparade M P, Trommer W E
出版信息
Biochim Biophys Acta. 1979 May 10;568(1):177-82. doi: 10.1016/0005-2744(79)90284-5.
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 the tighter binding of NADH to the heart type. In both isozymes the binding of the binding of the spin-labeled coenzyme itself is weaker than found for its structural components.
本文描述了NAD+及其结构成分的自旋标记衍生物与猪骨骼肌乳酸脱氢酶（L-乳酸：NAD+氧化还原酶，EC 1.1.1.27）的结合情况。与先前用心肌同工酶得到的结果（Wenzel, H.R., Pfleiderer, G., Trommer, W.E., Paschenda, K.和Redhardt, A. (1976) Biochim. Biophys. Acta 452,292 - 301）相反，与N6-SL-AMP相比，N6-SL-ADP的结合常数没有显著增加。这种不同的行为可以通过肌肉同工酶中谷氨酰胺-31被丙氨酸取代来解释，这被认为是NADH与心脏型结合更紧密的原因。在两种同工酶中，自旋标记辅酶本身的结合比其结构成分的结合更弱。
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