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以草酰乙酸为底物时猪心苹果酸脱氢酶的米氏常数（作者译）

[The Km of malate dehydrogenase from pig heart with oxaloacetate as substrate (author's transl)].

作者信息

Bergmeyer H U, Rozalskis G

出版信息

Z Klin Chem Klin Biochem. 1975 Nov;13(11):509.

PMID:1240703
Abstract

Km is necessary to calculate the conditions for indicator reactions in coupled enzymic assays. When malate dehydrogenase is used as an indicator enzyme for the assay of aspartate aminotransferase activity, its Km in relation to oxaloacetate is needed. Km (oxaloacetate) of commercially available mitochondrial malate dehydrogenase from pig heart was determined as Km equals 1.65 x 10(-5) mol/1 using the measurement conditions for aspartate aminotransferase according to the preliminary recommendations of the IFCC.

摘要

米氏常数（Km）对于计算偶联酶分析中指示反应的条件是必要的。当使用苹果酸脱氢酶作为测定天冬氨酸转氨酶活性的指示酶时，需要其相对于草酰乙酸的米氏常数。根据国际临床化学和检验医学联合会（IFCC）的初步建议，按照天冬氨酸转氨酶的测量条件，测定了市售猪心线粒体苹果酸脱氢酶的米氏常数（草酰乙酸），结果为米氏常数等于1.65×10⁻⁵摩尔/升。

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1
[The Km of malate dehydrogenase from pig heart with oxaloacetate as substrate (author's transl)].以草酰乙酸为底物时猪心苹果酸脱氢酶的米氏常数（作者译）
Z Klin Chem Klin Biochem. 1975 Nov;13(11):509.
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Enzyme-enzyme complexes between aspartate aminotransferase and malate dehydrogenase from pig heart muscle.
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[Effect of thyroxine on aspartate aminotransferase and malate dehydrogenase activity in guinea pig myocardium].[甲状腺素对豚鼠心肌中天冬氨酸转氨酶和苹果酸脱氢酶活性的影响]
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The anomalous kinetics of coupled aspartate aminotransferase and malate dehydrogenase. Evidence for compartmentation of oxaloacetate.天冬氨酸转氨酶与苹果酸脱氢酶偶联反应的异常动力学。草酰乙酸区室化的证据。
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Kinetics of the coupled aspartate aminotransferase-malate dehydrogenase reactions and instability of oxaloacetate on anion-exchange resin.
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Coupled reaction of immobilized aspartate aminotransferase and malate dehydrogenase. A plausible model for the cellular behaviour of these enzymes.固定化天冬氨酸转氨酶与苹果酸脱氢酶的偶联反应。这些酶细胞行为的一种合理模型。
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