Maita T, Araya A, Matsuda G, Goodman M
J Biochem. 1979 Jan;85(1):259-69. doi: 10.1093/oxfordjournals.jbchem.a132319.
Globin prepared from hemoglobin of the European hedgehog (Erinaceus europaeus) was separated into alpha and beta polypeptide chains by chromatography on a CM 52 column. The S-aminoethylated alpha and beta chains were each digested with trypsin and the resulting peptides were isolated. The sequences of all the tryptic peptides were established. The ordering of these peptides in the alpha and beta chains was deduced from their homology with the primary structures of alpha and beta chains of human adult hemoglobin. Comparing the primary structures of the alpha and beta chains of adult hemoglobin of the European hedgehog thus obtained with those of adult hemoglobin of the tupai (Tupaia glis), 35 amino acids substitutions in the alpha chains and 30 in the beta chains were recognized.
从欧洲刺猬(Erinaceus europaeus)血红蛋白制备的珠蛋白,通过在CM 52柱上进行色谱分离,被分成α和β多肽链。将S-氨乙基化的α链和β链分别用胰蛋白酶消化,并分离得到的肽段。确定了所有胰蛋白酶肽段的序列。根据这些肽段与成人血红蛋白α链和β链一级结构的同源性,推断它们在α链和β链中的排列顺序。由此获得的欧洲刺猬成人血红蛋白α链和β链的一级结构与树鼩(Tupaia glis)成人血红蛋白的一级结构进行比较,发现α链中有35个氨基酸替换,β链中有30个氨基酸替换。