一项关于两种蛋白质相互作用的研究，其中一种蛋白质含有黄素单核苷酸。

A study of the interaction between two proteins, one containing a flavin mononucleotide.

作者信息

Albani J

机构信息

Université des Sciences et Techniques de Lille, Laboratoire de Biophysique Moléculaire, Villeneuve d'Ascq, France.

出版信息

J Biochem Biophys Methods. 1993 May;26(2-3):105-12. doi: 10.1016/0165-022x(93)90040-u.

DOI:10.1016/0165-022x(93)90040-u

PMID:8389780

Abstract

Interaction between cytochrome c and flavocytochrome b2 has been studied in presence of 2-p-toluidinylnaphthalene-6-sulfonate (TNS). Affinity of the probe to flavocytochrome b2 increases when the complex between the two proteins is obtained. Binding of TNS increases the fluorescence of flavocytochrome b2 FMN. When the stoichiometry of the complex between the two proteins is reached, TNS looses its affinity and stops binding on the flavocytochrome b2; consequently, FMN fluorescence increase is no more observed. The dissociation constant of the complex was found equal to 0.1 microM. A similar result was obtained for the interaction between cytochrome c and flavodehydrogenase domain. The latter was obtained by proteolysis of flavocytochrome b2.

摘要

在2-对甲苯胺基萘-6-磺酸盐（TNS）存在的情况下，研究了细胞色素c与黄素细胞色素b2之间的相互作用。当获得两种蛋白质之间的复合物时，探针与黄素细胞色素b2的亲和力增加。TNS的结合增加了黄素细胞色素b2 FMN的荧光。当达到两种蛋白质之间复合物的化学计量时，TNS失去其亲和力并停止与黄素细胞色素b2结合；因此，不再观察到FMN荧光增加。发现该复合物的解离常数等于0.1微摩尔。细胞色素c与黄素脱氢酶结构域之间的相互作用也得到了类似的结果。后者是通过黄素细胞色素b2的蛋白水解获得的。