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人γ-谷氨酰羧化酶cDNA的克隆与表达

Cloning and expression of the cDNA for human gamma-glutamyl carboxylase.

作者信息

Wu S M, Cheung W F, Frazier D, Stafford D W

机构信息

Department of Biology, University of North Carolina, Chapel Hill 27599-3280.

出版信息

Science. 1991 Dec 13;254(5038):1634-6. doi: 10.1126/science.1749935.

Abstract

The cDNA for human gamma-glutamyl carboxylase, which accomplishes the post-translational modification required for the activity of all of the vitamin K-dependent proteins, was cloned. The enzyme is a 758-residue integral membrane protein and appears to have three transmembrane domains near its amino terminus. The hydrophilic COOH-terminal half of the carboxylase has 19.3 percent identity with soybean seed lipoxygenase. Expression of the cloned cDNA resulted in an increase in carboxylase activity in microsomes of transfected cells compared to mock-transfected cells.

摘要

完成所有维生素K依赖蛋白活性所需的翻译后修饰的人γ-谷氨酰羧化酶的cDNA被克隆出来。该酶是一种由758个氨基酸残基组成的整合膜蛋白,在其氨基末端附近似乎有三个跨膜结构域。羧化酶的亲水性羧基末端一半与大豆种子脂氧合酶有19.3%的同源性。与mock转染细胞相比,克隆的cDNA的表达导致转染细胞微粒体中羧化酶活性增加。

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