摘要
本文采用N—乙基顺丁烯二酰亚胺活化、Triton X—100增溶、羟基磷灰石和离子交换柱层析从Wistar大鼠肝脏中提纯了微粒体谷胱甘肽转移酶。SDS—聚丙烯酰胺凝胶电泳为一条带。氨基末端为丙氨酸。由不同角度鉴定酶制备物的纯度,认为它达到了均一,提纯倍数为28,回收率38％,比活性为15μmol·min^(-1)·mg^(-1),符合进一步进行性质研究的要求。它的最适pH为6.8,最适温度为30℃。
The rat liver microsomal glutathione transferase was activated by N-ethylmaleimide,solubilized by Triton X-100 and purified by chromatograghy on hydroxyapatite and CM Sephadex C-50.A 28-fold purification resulted in a 38% yield.The purified protein moved as a band with an apparent molecular weight of 14 000 on sodium dodcyl sulphate polyacrylamide gel electrophoresis and ap-peared to be nearly homogeneous.The N-terminal amino acid of the purified enzyme was alanine by the dansyl method.Optimum pH and temperature were 6.8 and 30℃,respectively.
出处
《中国药理学与毒理学杂志》
CAS
CSCD
北大核心
1990年第3期200-203,共4页
Chinese Journal of Pharmacology and Toxicology
基金
国家科学基金
关键词
谷胱甘肽
转移酶
微粒体
纯化
glutathione transferase
micro-some
liver
purification
