Maita T, Setoguchi M, Matsuda G, Goodman M
J Biochem. 1979 Mar;85(3):755-64.
Globin prepared from hemoglobin of the brown lemur (Lemur fulvus fulvus) was separated into alpha and beta chains by chromatography on a CM 52 column. The S-aminoethylated alpha and beta chains were each digested with trypsin and resulting peptides were isolated. The amino acid sequences of the tryptic peptides were established. The ordering of these peptides in the alpha and beta chains was deduced from the homology of their amino acid sequences with that of human adult hemoglobin. The primary structure of brown lemur hemoglobin thus obtained differs from that of human hemoglobin in 15 amino acids in the alpha chain and 26 in the beta chain.
从褐狐猴(Lemur fulvus fulvus)血红蛋白中制备的珠蛋白,通过在CM 52柱上进行色谱分离,被分成α链和β链。将S-氨乙基化的α链和β链分别用胰蛋白酶消化,并分离得到产生的肽段。确定了胰蛋白酶肽段的氨基酸序列。根据这些肽段与成人血红蛋白氨基酸序列的同源性,推断出它们在α链和β链中的排列顺序。由此获得的褐狐猴血红蛋白的一级结构与人类血红蛋白的一级结构相比,α链中有15个氨基酸不同,β链中有26个氨基酸不同。