Yano H, Satake K, Ueno Y, Kondo K, Tsugita A
Research Institute for Biosciences, Science University of Tokyo.
J Biochem. 1991 Sep;110(3):376-80. doi: 10.1093/oxfordjournals.jbchem.a123589.
The amino acid sequence of the alpha subunit of the allosteric hemerythrin from Lingula unguis was determined. It consists of 117 amino acid residues. Compared with other non-allosteric hemerythrins consisting of identical subunits of 113 amino acid residues, this protein has the deletion of the N-terminal amino acid and the insertion of five amino acids in the same region as in the case of the monomeric myoerythrin from Themiste zostericola. As the amino acid sequence of the beta subunit has also been determined [Yano, H., Satake, K., Ueno, Y., & Tsugita, A. Protein Sequence and Data Analysis, in press], the complete sequence analysis of an allosteric hemerythrin has been accomplished for the first time. The difference in the octameric structures of allosteric and non-allosteric hemerythrins are discussed.
测定了舌形贝变构血球素α亚基的氨基酸序列。它由117个氨基酸残基组成。与其他由113个氨基酸残基的相同亚基组成的非变构血球素相比，该蛋白质在与来自带纹铠茗荷儿的单体肌血球素相同的区域缺失了N端氨基酸并插入了五个氨基酸。由于β亚基的氨基酸序列也已确定[矢野，H.，笹武，K.，上野，Y.，& 津木田，A. 蛋白质序列与数据分析，即将出版]，首次完成了变构血球素的完整序列分析。讨论了变构和非变构血球素八聚体结构的差异。
