胰岛素诱导的鸡肝精氨酸酶的动力学特性及L-鸟氨酸对其的调节作用。

Kinetic properties and regulation by L-ornithine of chicken liver arginase induced by insulin.

作者信息

Bedino S, Testore G

出版信息

Hoppe Seylers Z Physiol Chem. 1979 Dec;360(12):1713-20. doi: 10.1515/bchm2.1979.360.2.1713.

DOI:10.1515/bchm2.1979.360.2.1713

Abstract

After injection of insulin into chickens, a new form of arginase with a 16-fold increase of activity appears in the liver. The new form has a different chromatographic behaviour on DEAE-cellulose. The low activity enzyme has a very high Km value (60mM), and is poorly inhibited by L-ornithine. The induced form of arginase is strongly inhibited by L-ornithine and has an allosteric behaviour which can be described by a Monod-Wyman-Changeux model. 1,4-Diaminobutane, spermine have practically no effect on either form of arginase.

摘要

给鸡注射胰岛素后，肝脏中会出现一种活性增加16倍的新型精氨酸酶。这种新形式在DEAE-纤维素上具有不同的色谱行为。低活性酶具有非常高的Km值（60mM），且受L-鸟氨酸的抑制作用较弱。诱导型精氨酸酶受到L-鸟氨酸的强烈抑制，并具有可用莫诺德-怀曼-尚热模型描述的别构行为。1,4-二氨基丁烷、精胺对两种形式的精氨酸酶实际上均无影响。