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[胃和胰腺黏膜支链氨基酸转氨酶的拓扑结构、理化性质及动力学特性]

[Topography, physicochemical and kinetic properties of the branched amino acid transaminases of the gastric and pancreatic mucosa].

作者信息

Bos S, Kostryrko V A, Berezov T T

出版信息

Vopr Med Khim. 1979 Sep-Oct;25(5):633-5.

PMID:494549
Abstract

About 40% of transaminase of branched amino acids were shown to be localized in mitochondrial matrix of pancreatic gland. The transaminases from pancreas and gastric mucosa had pH optima around pH 8.6. The enzymatic activity was increased with an increase in temperature to 50 degrees. In presence of 10 microM concentration of alpha-ketoglutarate Km volume of these two enzymes from postmitochondrial fraction of gastric mucosa and of pancreas were equal to 9.7 . 10(-4)M and 9.0 . 10(-4)M for leucine, 1.1.10(-4) M and 4.10(-3) M for valine, 6.4.10(-4) M and 8.5.10(-4) for isoleucine, respectively. The reaction or transamination proceeded via formation of a substituted form of the enzyme. The transaminase activity was inhibited by capronic acid (I506.8.10(-4) M), valeric acid (I508.10(-4)M), butyric acid (I50 5.8.10(-3) M) and propionic acid (I50 2.10(-2) M).

摘要

约40%的支链氨基酸转氨酶定位于胰腺的线粒体基质中。来自胰腺和胃黏膜的转氨酶的最适pH值约为8.6。酶活性随温度升高至50摄氏度而增加。在存在10微摩尔浓度的α-酮戊二酸时,来自胃黏膜和胰腺线粒体后部分的这两种酶对亮氨酸的Km值分别等于9.7×10⁻⁴M和9.0×10⁻⁴M,对缬氨酸分别为1.1×10⁻⁴M和4×10⁻³M,对异亮氨酸分别为6.4×10⁻⁴M和8.5×10⁻⁴M。转氨反应通过形成酶的取代形式进行。转氨酶活性受到己酸(I50 6.8×10⁻⁴M)、戊酸(I50 8×10⁻⁴M)、丁酸(I50 5.8×10⁻³M)和丙酸(I50 2×10⁻²M)的抑制。

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