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将鸟氨酸转氨酶前体导入线粒体所必需的受体蛋白的部分纯化。

Partial purification of the receptor protein essential for import of pre-ornithine aminotransferase into mitochondria.

作者信息

Ono H, Tuboi S

出版信息

Biochem Int. 1985 Mar;10(3):351-7.

PMID:4015663
Abstract

The isolated mitochondrial outer membrane fraction strongly inhibits the import of pre-ornithine aminotransferase, but other membranes such as rough microsomes did not. This inhibition seems to be caused by a receptor in the isolated outer membrane which binds competitively pre-ornithine aminotransferase. The mitochondrial outer membrane could be solubilized using detergent. And a receptor for pre-ornithine aminotransferase was partially purified by ammonium sulfate fractionation followed by column chromatography on Sephacryl S-300. Liposomes reconstituted from the partially purified receptor and lecithin could inhibit the import of pre-ornithine aminotransferase into mitochondria and bind the precursor.

摘要

分离得到的线粒体外膜组分强烈抑制鸟氨酸转氨酶前体的导入,但其他膜结构如糙面微粒体则无此作用。这种抑制作用似乎是由分离的外膜中的一种受体引起的,该受体与鸟氨酸转氨酶前体竞争性结合。线粒体外膜可用去污剂溶解。通过硫酸铵分级分离,然后在Sephacryl S - 300上进行柱层析,部分纯化了鸟氨酸转氨酶前体的受体。由部分纯化的受体和卵磷脂重构的脂质体能够抑制鸟氨酸转氨酶前体导入线粒体并结合该前体。

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Biochem Int. 1985 Mar;10(3):351-7.
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