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氯化钠溶液中乳酸脱氢酶的H4同工酶——3. 酶活性与丙酮酸抑制作用

H4-isozyme of lactate dehydrogenase in the solution of sodium chloride--3. The enzymatic activity and the pyruvate inhibition.

作者信息

Yamamoto S

出版信息

Int J Biochem. 1983;15(2):185-90. doi: 10.1016/0020-711x(83)90064-2.

DOI:10.1016/0020-711x(83)90064-2
PMID:6822318
Abstract
  1. Low enzymatic activities in low pyruvate concentrations and high Km were observed in sodium chloride solutions. 2. The pyruvate inhibition shown by the % activity at 1 mM pyruvate was lower sodium chloride than in 0.1 M sodium phosphate. 3. At 40 degrees C, as compared with results at 20 degrees C, less pyruvate inhibition was observed in phosphate buffer and in sodium chloride solutions. 4. By using the equilibrium constants between dimer and tetramer, a theoretical explanation is proposed for the pyruvate inhibition. In this explanation, it is suggested that the quaternary complex which is composed of tetrameric enzyme, coenzyme and two kinds of pyruvates was the main cause of the pyruvate inhibition.
摘要
  1. 在氯化钠溶液中观察到丙酮酸浓度较低时酶活性较低且米氏常数较高。2. 在1 mM丙酮酸浓度下,与0.1 M磷酸钠相比,氯化钠溶液中丙酮酸抑制作用所表现出的活性百分比更低。3. 在40℃时,与20℃时的结果相比,在磷酸盐缓冲液和氯化钠溶液中观察到的丙酮酸抑制作用较小。4. 通过使用二聚体和四聚体之间的平衡常数,对丙酮酸抑制作用提出了一种理论解释。在此解释中,认为由四聚体酶、辅酶和两种丙酮酸组成的四级复合物是丙酮酸抑制作用的主要原因。

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