Suzuki T, Yasunaga H, Furukohri T, Nakamura K, Gotoh T
J Biol Chem. 1985 Sep 25;260(21):11481-7.
The giant extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus consists of two types of subunits: a "monomeric" chain (chain I) and a disulfide-bonded trimer of chains IIA, IIB, and IIC. The complete amino acid sequence of chain IIB was determined. This chain has 148 amino acid residues and a molecular weight of 17,236 including a heme group. Of the residues in chain IIB, 74 (50%) and 34 (30%) were found to be identical with those in the corresponding positions in Tylorrhynchus chains IIC and I, respectively (Suzuki, T., Furukohri, T., and Gotoh, T. (1985) J. Biol. Chem. 260, 3145-3154). Marked differences were found between the chains of Tylorrhynchus and Lumbricus in the COOH-terminal regions. Significant differences were predicted between the monomeric chain I and the "trimeric" chains (IIB and IIC) in the hydropathy profiles and alpha-helical contents.
一条“单体”链（I链）和由IIA、IIB和IIC链通过二硫键连接而成的三聚体。确定了IIB链的完整氨基酸序列。该链有148个氨基酸残基，分子量为17236，包括一个血红素基团。发现IIB链中的74个残基（50%）和34个残基（30%）分别与异足索沙蚕IIC链和I链相应位置的残基相同（铃木，T.，古堀里，T.，和后藤，T.（1985年）《生物化学杂志》260，3145 - 3154）。在异足索沙蚕和蚯蚓的链的COOH末端区域发现了明显差异。预测单体I链与“三聚体”链（IIB和IIC）在亲水性图谱和α - 螺旋含量方面存在显著差异。
