ISSN:
1432-136X
Keywords:
Multiple hemoglobins
;
Subunit structure
;
α-chain
;
β-chain
;
Carp, Cyprinus carpio
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00346928
