大鼠心脏主要的谷胱甘肽S-转移酶是由Yb大小的亚基组成的阴离子同工酶。

The major rat heart glutathione S-transferases are anionic isozymes composed of Yb size subunits.

作者信息

Tu C P, Chang M, Reddy C C

出版信息

Biochem Biophys Res Commun. 1984 Sep 28;123(3):981-8. doi: 10.1016/s0006-291x(84)80230-2.

Abstract

The GSH S-transferases from rat heart cytosol has been purified by S-hexylglutathione-linked Sepharose-6B affinity chromatography. The majority (approximately 80%) of these GSH S-transferases are anionic isozymes which can be resolved further by DEAE-cellulose column chromatography and isoelectric focusing. They are mainly composed of Yb size (Mr = 27,000) subunits with different substrate specificity patterns from the rat liver anionic GSH S-transferases. The major cationic GSH S-transferases from liver are not expressed in rat heart. Although some cationic GSH S-transferases from rat heart can be purified by CM-cellulose column chromatography they are composed of major subunits of Yb electrophoretic mobility.

摘要

大鼠心脏胞液中的谷胱甘肽S-转移酶已通过S-己基谷胱甘肽连接的琼脂糖凝胶6B亲和层析法纯化。这些谷胱甘肽S-转移酶中的大多数（约80%）是阴离子同工酶，可通过DEAE-纤维素柱层析和等电聚焦进一步分离。它们主要由Yb大小（Mr = 27,000）的亚基组成，其底物特异性模式与大鼠肝脏阴离子谷胱甘肽S-转移酶不同。肝脏中的主要阳离子谷胱甘肽S-转移酶在大鼠心脏中不表达。尽管大鼠心脏中的一些阳离子谷胱甘肽S-转移酶可通过CM-纤维素柱层析纯化，但它们由具有Yb电泳迁移率的主要亚基组成。