Suzuki T, Gotoh T
J Mol Biol. 1986 Jul 5;190(1):119-23. doi: 10.1016/0022-2836(86)90081-1.
The subunit assembly of the giant haemoglobin of the polychaete Tylorrhynchus heterochaetus is presented. Tylorrhynchus haemoglobin consists of two types of subunits: a "monomeric" chain I and a disulphide-bonded "trimer" of chains IIA, IIB and IIC. The molar ratio of the four constituent chains was determined by statistical comparison of the accurate amino acid composition calculated from the sequence of each chain and the observed composition measured by amino acid analysis of the whole molecule. On the basis of the molar ratio and the molecular weight of each chain, deduced from the amino acid sequence, a symmetrical model for the molecular assembly of the haemoglobin was constructed. The proposed model consists of four species of chains of 192 polypeptides and has a molecular weight of 3,275,808. The minimum structural entity is a "tetramer" consisting of the "monomeric" chain and the disulphide-bonded "trimer". Each chain contains one haem.
本文介绍了多毛纲动物异毛虫（Tylorrhynchus heterochaetus）巨型血红蛋白的亚基组装情况。异毛虫血红蛋白由两种类型的亚基组成：“单体”的I链和通过二硫键连接的由IIA、IIB和IIC链组成的“三聚体”。通过对根据每条链的序列计算出的精确氨基酸组成与通过对整个分子进行氨基酸分析测得的观察组成进行统计比较，确定了四种组成链的摩尔比。根据从氨基酸序列推导得出的每条链的摩尔比和分子量，构建了血红蛋白分子组装的对称模型。所提出的模型由192个多肽的四种链组成，分子量为3,275,808。最小的结构实体是由“单体”链和通过二硫键连接的“三聚体”组成的“四聚体”。每条链都含有一个血红素。
