[人脑海马体谷氨酸脱羧酶的纯化]

[Purification of the glutamate decarboxylase from human brain].

作者信息

Blindermann J M, Maître M, Ossola L, Mandel P

出版信息

C R Acad Hebd Seances Acad Sci D. 1977 Oct 24;285(10):1079-82.

Abstract

A method of purifying the glutamate decarboxylase from human brain is described. The enzyme was purified 8 000 fold in regard to the initial homogenate and appears homogenous by electrophoresis, both in denaturing and non-denaturing conditions. The molecular weight of the native enzyme and its subunits indicate that GAD from human brain is formed by two similar if non identical polypeptide chains. The Km for glutamate and pyridoxal phosphate found for the human enzyme, respectively 1,2.10(-3) M and 0,13.10(-6) M, are close to the Km found for the Mouse enzyme.

摘要

本文描述了一种从人脑中纯化谷氨酸脱羧酶的方法。相对于初始匀浆，该酶被纯化了8000倍，并且在变性和非变性条件下通过电泳均显示为均一性。天然酶及其亚基的分子量表明，人脑中的谷氨酸脱羧酶由两条相似（若非完全相同）的多肽链组成。人源酶的谷氨酸和磷酸吡哆醛的米氏常数分别为1.2×10⁻³ M和0.13×10⁻⁶ M，与小鼠酶的米氏常数相近。