Abstract
Three hemoglobin components in carp designated CI, CII, and CIII, were isolated by DEAE-Toyopearl ion-exchange chromatography. Constituent globin chains, α1, α2, β1 and β2, were analyzed by urea-Triton acid polyacrylamide gel electrophoresis and isolated by high performance liquid chromatography with a reversed-phase column. Tryptic peptide mapping indicated that the α-globin chains of the three hemoglobin components have slightly different structures. In addition, N-terminal amino acid sequence analysis indicated that the β1-globin chain has a primary structure different from that of the β2-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 (α1 α2 β 2 1 ), CII (α1 α2 β1 β2), and CIII (α1 α2 β 2 2 ). Hemoglobin CII was a hybrid between the two types each of α- and β-chain and could be constructed in vitro from two hemoglobin components CI and CIII.
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