[Hemoglobins, XXXV: The sequence of the beta A- und beta B-Chains of the hemoglobins of the carp (Cyprinus carpio L.)].

The primary structure of the beta A- and beta B-chains from both main components of the tetrameric hemoglobins from carp is given. The sequences were found by automatic analysis in the sequenator using a hydrophilic and hydrophobic program with hydrophilic isothiocyanate. The beta-chains A and B differ in positions beta 13, beta 41, beta 122 and beta 143. In comparison to human beta-chains carp beta A- and beta B-chains show 66 and 67 residues, respectively (45%). Furthermore, we found one insertion in the GH-region, therefore the chains contain 147 amino acids. The sequence is discussed and in particular, the chains of tetrameric hemoglobins are compared to those of mammalia: beta A and beta B contain 3 and 4 cysteines, respectively, but the external cysteine beta 93 of mammalia is replaced by serine. In ;the N-terminal region in E-helix and G-helix an accumulation of mutations is found. Furthermore, we think the high oxidation of the hemoglobins from carp comes from an external cysteine in beta 31 and beta 143, respectively. Several aspects of an ATP-hemoglobin exchange and its function are discussed.