Effects of halides on reduced nicotinamide adenine dinucleotide binding properties and catalytic activity of beef heart lactate dehydrogenase.
Effects of halides on reduced nicotinamide adenine dinucleotide binding properties and catalytic activity of beef heart lactate dehydrogenase.
复制标题
卤化物对还原烟酰胺腺嘌呤二核苷酸结合特性和牛心乳酸脱氢酶催化活性的影响。
DOI：
10.1021/bi00506a003
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Anderson,SR
中科院分区：
文献类型：
--
作者：
Anderson,SR
材料与方法NADH和丙酮酸钠从Sigma Chemical Co.获得。所有其他化学品均为试剂级。通过使用去离子玻璃蒸馏水制备溶液。在整个实验中使用相同的缓冲液，0.05 M磷酸钾，pH 7.4。纯化的H4同工酶是从Worthington Biochemical Corp.的牛心乳酸脱氢酶制备物中层析分离的。（Pesce等人，1964年）。催化活性所有速率测量均为在卡里15分光光度计上在340 nm处测定的初始反应速度。检测了丙酮酸和NADH在其相应Km范围内的浓度。比色皿
Materials and MethodsReagents. NADH and sodium pyruvate were obtained from Sigma Chemical Co. All other chemicals were reagent grade. Solutions were prepared by using deionized glass-distilled water. The same buffer, 0.05 M potassium phosphate at pH 7.4, was used throughout the experiments. The pureH4 isozyme was isolated chromatographically from a preparation of beef heart lactic dehydrogenase obtained from Worthington Biochemical Corp.(Pesce et al., 1964). Catalytic Activity. All rate measurements were initial re-action velocities determined at 340 nm on a Cary 15 spec-trophotometer. Concentrations of pyruvate and NADH in the range of their corresponding Km’s were examined. Cuvettes