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多毛纲动物杂毛虫巨型多亚基血红蛋白的完整氨基酸序列。

The complete amino acid sequence of giant multisubunit hemoglobin from the polychaete Tylorrhynchus heterochaetus.

作者信息

Suzuki T, Gotoh T

出版信息

J Biol Chem. 1986 Jul 15;261(20):9257-67.

PMID:3722198
Abstract

The extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus is a "giant," multisubunit protein with an apparent molecular weight of 3.37 X 10(6), and consists of two types of subunits: a "monomeric" chain (chain I) and a disulfide-bonded "trimer" of chains IIA, IIB, and IIC. We reported the amino acid sequences of chains I, IIB, and IIC previously (Suzuki, T., Yasunaga, H., Furukohri, T., Nakamura, K., and Gotoh, T. (1985) J. Biol. Chem. 260, 11481-11487). The sequence of chain IIA has now been determined. Chain IIA consists of 146 amino acid residues with a heme group and has a molecular weight of 17,236. All of the constituent chains of Tylorrhynchus hemoglobin appear to be homologous with those of vertebrate hemoglobins and contain heme. Distal (E7) His, distal (E11) Val, and proximal (F8) His are all conserved in the four chains. Phylogenetically, chain IIA appears more closely related to the monomeric chain I than to either of the other "trimeric" chains IIB and IIC. This is the first giant extracellular hemoglobin to be sequenced completely.

摘要

多毛纲动物异足索沙蚕的细胞外血红蛋白是一种“巨型”多亚基蛋白，表观分子量为3.37×10⁶，由两种亚基组成：一种“单体”链（I链）和一种由IIA链、IIB链和IIC链通过二硫键连接而成的“三聚体”。我们之前报道了I链、IIB链和IIC链的氨基酸序列（铃木，T.，安永，H.，古越，T.，中村，K.，和后藤，T.（1985年）《生物化学杂志》260，11481 - 11487）。现在已经确定了IIA链的序列。IIA链由146个氨基酸残基组成，带有一个血红素基团，分子量为17,236。异足索沙蚕血红蛋白的所有组成链似乎都与脊椎动物血红蛋白的链同源，并且都含有血红素。远端（E7）组氨酸、远端（E11）缬氨酸和近端（F8）组氨酸在这四条链中均保守。从系统发育角度来看，IIA链与单体I链的关系似乎比与其他“三聚体”链IIB和IIC中的任何一条都更为密切。这是第一个被完全测序的巨型细胞外血红蛋白。

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