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角鲨烯合成酶的纯化至均一性及其某些性质

Purification to homogeneity and some properties of squalene synthetase.

作者信息

Sasiak K, Rilling H C

机构信息

Department of Biochemistry, University of Utah School of Medicine, Salt Lake City 84108.

出版信息

Arch Biochem Biophys. 1988 Feb 1;260(2):622-7. doi: 10.1016/0003-9861(88)90490-0.

DOI:10.1016/0003-9861(88)90490-0
PMID:3277535
Abstract

Squalene synthetase has been purified to homogeneity from yeast. It is a single polypeptide of Mr 47,000. This enzyme catalyzes the synthesis of squalene from farnesyl diphosphate via presqualene diphosphate. In the presence of reduced pyridine nucleotides, presqualene diphosphate and squalene are produced in a ratio of 6:1 from either the purified protein or the crude microsomal fraction.

摘要

角鲨烯合酶已从酵母中纯化至同质。它是一种分子量为47,000的单一多肽。该酶催化从法呢基二磷酸经前角鲨烯二磷酸合成角鲨烯。在还原型吡啶核苷酸存在的情况下,无论是纯化的蛋白质还是粗微粒体部分,前角鲨烯二磷酸和角鲨烯的生成比例均为6:1。

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