Naqvi S, Abbasi A, Zaidi Z H
H.E.J. Research Institute of Chemistry, University of Karachi, Pakistan.
J Protein Chem. 1994 Nov;13(8):669-79. doi: 10.1007/BF01886951.
Cobra snake Naja naja naja hemoglobin shows four bands on Triton electrophoresis. We present the primary structure of one alpha and one beta chain. The separation of polypeptide chains was achieved by ion exchange chromatography on carboxymethyl cellulose column. The amino acid sequence was established by automatic Edman degradation of the native chains and tryptic and hydrolytic peptides in a gas-phase sequencer. The structural data are compared with those of human and other reptile hemoglobins and reveal not only large variations from human but within reptiles. The amino acid exchanges involve several subunit contacts and heme binding sites. This is the first study on the hemoglobin of a land snake. There are only two amino acid sequences of sea snake hemoglobin (Microcephalophis gracilis gracilis and Liophis miliaris) reported in the literature.
眼镜蛇印度眼镜蛇的血红蛋白在Triton电泳上显示出四条带。我们给出了一条α链和一条β链的一级结构。通过在羧甲基纤维素柱上进行离子交换色谱法实现了多肽链的分离。氨基酸序列是通过在气相测序仪中对天然链以及胰蛋白酶和水解肽进行自动埃德曼降解来确定的。将结构数据与人类和其他爬行动物的血红蛋白数据进行比较，结果表明不仅与人类血红蛋白有很大差异，而且在爬行动物内部也存在差异。氨基酸交换涉及几个亚基接触点和血红素结合位点。这是对陆生蛇血红蛋白的首次研究。文献中仅报道了两种海蛇血红蛋白（细纹小头海蛇和多带丽蛇）的氨基酸序列。
