title: Subunit structure of multiple hemoglobins in carp.
abstract: Three hemoglobin components in carp designated CI, CII, and CIII, were isolated by DEAE-Tokyo-pearl ion-exchange chromatography. Constituent globin chains, alpha 1, alpha 2, beta 1, and beta 2, were analyzed by urea-Triton acid polyacrylamide gel electrophoresis and isolated by high performance liquid chromatography with a reverse-phase column. Tryptic peptide mapping indicated that the alpha-globin chains of the three hemoglobin components have slightly different structures. In addition, N-terminal amino acid sequence analysis indicated that the beta 1-globin chain has a primary structure different from that of the beta 2-chain. A series of hybridization experiments between isolated hemoglobins, together with such structural properties of globin chains, suggested that the three hemoglobins have the following compositions: CI (alpha 1  alpha 2 beta 1(2)), CII (alpha 1 alpha 2 beta 1 beta 2), and CIII (alpha 1 alpha 2 beta 2(2)). Hemoglobin CII was a hybrid between the two types each of alpha- and beta-chain and could be constructed in vitro from two hemoglobin components CI and CIII.
authors.affiliation: Laboratory of Sea-Farming, Tokyo University of Fisheries, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Ohkudo
authors.forename: S
authors.initials: S
authors.lastname: Watabe
authors.forename: T
authors.initials: T
authors.lastname: Oshiro
authors.forename: F
authors.initials: F
authors.lastname: Takashima
authors.forename: H
authors.initials: H
authors.lastname: Nakajima
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002347:Carps / Q000097:blood*; D002851:Chromatography, High Pressure Liquid; D005914:Globins / Q000737:chemistry; D006454:Hemoglobins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010449:Peptide Mapping
chemical_list: D006454:Hemoglobins; D005914:Globins