No abstract

Complete amino acid sequences of lion (Panthera leo) hemoglobins are reported. Polyacrylamide gel disc electrophoresis at pH 8.3 and also in the presence of 8 M urea and Triton-X100, RP-HPLC, liquid and gas phase amino acid sequenator. and FAB Mass spectrometer are used. Sequences are aligned with human hemoglobin (Hb A ) and compared with other hemoglobins of felidae.

The complete primary structure of the hemoglobin from the adult coati (Nasua nasua rufa) is presented. The erythrocytes contain one hemoglobin component and two globin chains. The isolation of globin chains was achieved by reversed-phase HPLC on a column of Nucleosil-C4. The primary structures of globin chains and tryptic peptides was determined in liquid- and gas-phase sequenators. The sequence of the alpha and beta-chains of coati compared with those of other Carnivora species. Results are discussed with respect to structural variations and the phylogenetic relationship.

The complete amino acid sequences of the hemoglobins from the adult European polecat (Mustela putorius) are presented. The erythrocytes contain two hemoglobin components and three globin chains (α I, α II and β). The primary structure of globin chains and of the tryptic peptides determined in liquid- and gas-phase sequantors. Comparing the sequences of the globin chains of the polecat with that of human Hb-A, 17 (23.9%) substitutions were recognized in the α I, 16 (22.5%) in the α II and 14 (20.4%) in the β chain. A high degree of homology observed with other representatives of the family Mustelidae.

The complete primary structure of the two hemoglobin components of the fur seal (Arctocephalus galapagoensis) is presented. The two components (HbI and HblI) occur in nearly equal amounts and have identical ]3-chains; whereas the two a-chains (aI/alI) differ by six exchanges Ile/Val, Met/Thr, Ser/Ala, Pro/His, Lys/Gly, and Thr/Ala at positions 10, 34, 35, 50, 78, and 131, respectively. The components were isolated by DEAE-Sephacel chromatography and were separated into the globin chains by RP-HPLC on a column of Nucleocil-C4. The sequences have been determined by Edman degradation in liquid-and gas-phase sequencer, using the native chains and tryptic peptides. The sequences compared with those of other Carnivora species and an adult human globin chains. An identical ]3-chain is found in fur seal and walrus, whereas larger differences were found between aI and aII compared to ]3-chains.