多毛纲沙蚕的小镉结合蛋白（MP II）的氨基酸序列。肌红血球素结构的证据。

Amino acid sequence of the small cadmium-binding protein (MP II) from Nereis diversicolor (annelida, polychaeta). Evidence for a myohemerythrin structure.

作者信息

Demuynck S, Li K W, Van der Schors R, Dhainaut-Courtois N

机构信息

ERS 20 CNRS (Phylogénie moléculaire des Annélides), Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France.

出版信息

Eur J Biochem. 1993 Oct 1;217(1):151-6. doi: 10.1111/j.1432-1033.1993.tb18230.x.

DOI:10.1111/j.1432-1033.1993.tb18230.x

PMID:8223553

Abstract

The primary sequence of the low-molecular-mass cadmium-binding protein metalloprotein II of Nereis diversicolor (Hediste diversicolor, recent denomination) has been determined. This protein is composed of 119 amino acids and has 80.8% identity with the N. diversicolor myohemerythrin [Takagi, T. & Cox, J. A. (1991) FEBS Lett. 285, 25-27]. The fact that iron, which normally binds to myohemerythrin, is not found to be associated with the cadmium-binding protein metalloprotein II in cadmium-exposed animals could be the result of the complete abolition of the iron-binding capacity of the protein due to the binding of cadmium.

摘要

已测定多毛纲沙蚕（现称多变钩沙蚕）低分子量镉结合蛋白金属蛋白II的一级序列。该蛋白由119个氨基酸组成，与多变钩沙蚕的肌红血球素具有80.8%的同一性[高木，T. & 考克斯，J. A.（1991年）《欧洲生物化学学会联合会快报》285，25 - 27]。在接触镉的动物中，通常与肌红血球素结合的铁未被发现与镉结合蛋白金属蛋白II相关，这一事实可能是由于镉的结合导致该蛋白的铁结合能力完全丧失的结果。