PRIMARY STRUCTURE OF MYOHEMERYTHRIN FROM THE ANNELID NEREIS-DIVERSICOLOR

被引：19

作者：

TAKAGI, T ^{[1
]}

COX, JA ^{[1
]}

机构：

[1] UNIV GENEVA,DEPT BIOCHEM,CH-1211 GENEVA 4,SWITZERLAND

来源：

FEBS LETTERS | 1991年 / 285卷 / 01期

关键词：

MYOHEMERYTHRIN; ANNELID; PRIMARY STRUCTURE;

D O I：

10.1016/0014-5793(91)80716-G

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The metal-free form of Nereis diversicolor myohemerythrin was purified from whole animal extracts by trichloroacetic acid precipitation and ion exchange chromatography. The amino acid sequence of myohemerythrin has been determined. The protein is composed of 120 residues, possesses an unblocked N-terminus and is devoid of cysteine residues. It bears 62% sequence identity with Themiste zostericola myohemerythrin, the only other member of this subfamily sequenced to date. Within the family of hemerythrins, homology is particularly high in the segments involved in the binding of the two iron atoms and in the beta-turn-rich N-terminal segment.

引用

页码：25 / 27

页数：3

共 10 条

[1] CHARACTERIZATION OF A NEW SARCOPLASMIC CALCIUM-BINDING PROTEIN WITH MAGNESIUM-INDUCED COOPERATIVITY IN THE BINDING OF CALCIUM [J].