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胰岛素可激活鸟苷5'-[γ-硫代]三磷酸(GTPγS)与一种来自人胎盘的新型GTP结合蛋白GIR的结合。

Insulin activates guanosine 5'-[gamma-thio] triphosphate (GTP gamma S) binding to a novel GTP-binding protein, GIR, from human placenta.

作者信息

Srivastava S K, Singh U S

机构信息

Department of Human Biological Chemistry & Genetics, University of Texas Medical Branch, Galveston 77550.

出版信息

Biochem Biophys Res Commun. 1990 Dec 14;173(2):501-6. doi: 10.1016/s0006-291x(05)80062-2.

Abstract

A novel GTP-binding protein, GIR, along with insulin receptor (IR), has been partially purified from human placenta. A non-hydrolyzable substrate, GTP gamma S which is known to bind to GTP-binding proteins with high affinity, reduces insulin binding to IR-GIR fraction by approximately 29% and 100 nM insulin stimulates GTP gamma S binding to IR-GIR fraction by approximately five-fold. The molecular weight of the protein (may be subunit) that binds to 8-azido-GTP, a photoaffinity label for G-proteins, is approximately 66,000.

摘要

一种新型的GTP结合蛋白GIR,与胰岛素受体(IR)一起,已从人胎盘中部分纯化出来。一种已知能与GTP结合蛋白高亲和力结合的不可水解底物GTPγS,可使胰岛素与IR-GIR组分的结合减少约29%,而100 nM胰岛素可使GTPγS与IR-GIR组分的结合增加约五倍。与G蛋白的光亲和标记物8-叠氮基-GTP结合的蛋白质(可能是亚基)的分子量约为66,000。

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