Maita T, Tanaka E, Goodman M, Matsuda G
J Biochem. 1977 Aug;82(2):603-5.
Globin prepared from hemoglobin of adult tupai (Tupaia glis) was separated into alpha and beta polypeptide chains by CM-cellulose column chromatography. The S-aminoethylated alpha polypeptide chain and S-carboxymethylated beta polypeptide chain were each digested with trypsin, and the sequences of all the peptides thus obtained were established. The ordering of these tryptic peptides in the alpha and beta polypeptide chains was deduced from the homology of their primary structures with that of human adult hemoglobin. In this way the primary structures of the alpha and beta polypeptide chains of tupai hemoglobin were established; 27 amino acids in the alpha polypeptide chain and 26 in the beta chain differ from those in human adult hemoglobin.
从成年树鼩(笔尾树鼩)血红蛋白制备的珠蛋白,通过CM - 纤维素柱色谱法分离为α和β多肽链。对S - 氨乙基化的α多肽链和S - 羧甲基化的β多肽链各自用胰蛋白酶进行消化,并确定由此获得的所有肽段的序列。根据这些胰蛋白酶肽段与成人血红蛋白一级结构的同源性,推断它们在α和β多肽链中的排列顺序。通过这种方式确定了树鼩血红蛋白α和β多肽链的一级结构;α多肽链中有27个氨基酸,β多肽链中有26个氨基酸与成人血红蛋白中的不同。