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来自发光细菌费氏弧菌的核黄素结合蛋白。纯化与特性鉴定。

Lumazine protein from the bioluminescent bacterium Photobacterium phosphoreum. Purification and characterization.

作者信息

Small E D, Koka P, Lee J

出版信息

J Biol Chem. 1980 Sep 25;255(18):8804-10.

PMID:7410396
Abstract

Lumazine protein, a novel protein containing 6,7-dimethyl-8-ribityllumazine as a bound prosthetic group, is one of the several major proteins produced by the bioluminescent bacteria, Photobacterium phosphoreum. purification to complete homogeneity from cell extracts is achieved in six steps. Lumazine protein is a near spherical, monomeric protein of average molecular weight 20,000; in amino acid composition it is acidic with two isoelectric isomers, pI 4.9 and 5.0, and is hydrophilic (974 cal/residue) with single methionine and tryptophan residues and two accessible cysteines. It contains no carbohydrate. Reaction of the cysteines with dithionitrobenzoic acid results in quenching of the bound lumazine fluorescence but is otherwise reversible. Estimates of protein by dry weight results in a mole ratio of one bound lumazine group per protein.

摘要

核黄素蛋白是一种新型蛋白质,含有6,7 - 二甲基 - 8 - 核糖基核黄素作为结合辅基,是发光细菌磷光弧菌产生的几种主要蛋白质之一。通过六个步骤可从细胞提取物中纯化至完全同质。核黄素蛋白是一种近似球形的单体蛋白,平均分子量为20,000;在氨基酸组成上呈酸性,有两种等电异构体,pI为4.9和5.0,具有亲水性(974卡/残基),含有单个甲硫氨酸和色氨酸残基以及两个可及的半胱氨酸。它不含碳水化合物。半胱氨酸与二硫代硝基苯甲酸反应会导致结合的核黄素荧光猝灭,但在其他方面是可逆的。通过干重估算蛋白质得出每个蛋白质一个结合核黄素基团的摩尔比。

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J Biol Chem. 1980 Sep 25;255(18):8804-10.
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