CONFORMATIONAL-CHANGES IN ALLOSTERIC INHIBITION OF MUSCLE PYRUVATE-KINASE BY PHENYLALANINE
CONFORMATIONAL-CHANGES IN ALLOSTERIC INHIBITION OF MUSCLE PYRUVATE-KINASE BY PHENYLALANINE
复制标题
DOI：
10.1021/bi00773a031
复制
发表时间：
1972-01-01
期刊：
影响因子：
2.9
通讯作者：
PRICE, NC
中科院分区：
文献类型：
--
作者：
KAYNE, FJ;PRICE, NC
材料和方法根据Tietz 和Ochoa (1958)的方法从冷冻兔肌肉(Pel-Freeze，Rogers，Ark.)分离丙酮酸激酶。在最佳底物浓度和 pH 7.5 (= 24.5) 下，该制剂的比活性为每分钟每毫克蛋白质形成 250 µ 68 的产物。使用偶联乳酸脱氢酶测定法测定酶活性（Kayne，1971）。使用已发表的 280 nm 消光系数值和分子量通过分光光度法测定丙酮酸激酶浓度（Boyer，1962）。
Materials and MethodsPyruvate kinase was isolated from frozen rabbit muscle (Pel-Freeze, Rogers, Ark.) according to the method of Tietz and Ochoa (1958). The preparation had a specific activity of 250 µ 68 of product formed per min per mg of protein at optimal substrate concentrations and at pH 7.5 (= 24.5). Enzyme activity was assayed using the coupled lactate dehydrogenase assay (Kayne, 1971). Pyruvate kinase concentra-tions were determined spectrophotometrically using published values of the extinction coefficient at 280 nm and molecular weight (Boyer, 1962).