Purification and structure of the polypeptide chains of earthworm hemoglobin.
Purification and structure of the polypeptide chains of earthworm hemoglobin.
复制标题
蚯蚓血红蛋白多肽链的纯化及结构。
DOI：
10.1016/0003-9861(81)90545-2
复制
发表时间：
1981
影响因子：
3.9
通讯作者：
A. Riggs
中科院分区：
文献类型：
--
作者：
R. Garlick;A. Riggs
Carboxyhemoglobin from the earthworm,Lumbricus terrestris, separates on isoelectric focusing into a major component A, and a minor component B, which comprises 4–9% of the total. The molecular weights of all the polypeptide chains from either component have been estimated to be near 15,000–16,000 by chromatography on Sephacryl S-200 in 6mguanidine-HCl after oxidation with performic acid. Species of higher molecular weight were not detected under these conditions. The chains remain partially aggregated, however, in 8murea. Electrophoresis in 8murea at pH 3.5 on disc gels results in the separation of four protein bands. Analysis of chromatography of either globin A or B on carboxymethylcellulose in 8murea indicates that three of these bands are unique polypeptides chains. The fourth, most anodic, band appears to be a product of aggregation and not a unique polypeptide chain. The amino acid composition has been determined for the three chains isolated from each component. The NH2-terminal residues for the three isolated chains of globin A have been determined to be aspartic acid, alanine, and lysine. The unfractionated globin and that from components A and B have the same NH2termini.
