Hämoglobine, XLIV. Perissodactyla: Die Sequenz der Hämoglobine von Wildesel(Equus hemionus kulan)und Zebra(Equus zebra)

Abstract

The Hb from an asiatic wild ass (E. h. kulan) and a mountain zebra (E. zebra) were analyzed and the complete primary structure of the .alpha. and .beta. chains are described. The wild ass globin was separated in 2 .alpha. chains (.alpha.I and .alpha.II) and 1 .beta.-chain by means of chromatography on CM[carboxymethyl]-cellulose in 8 M urea buffer at pH 6.5. The wild ass globin shows polymorphism in the .alpha.-chain like the horse Hb. Under the same chromatographic conditions only 1 .alpha. and 1 .beta.-chain were found in the zebra globin. The primary structures were determined with the aid of an automatic liquid phase sequenator. There is only 1 amino acid differing between the .alpha.I- and .alpha.II-chain of wild ass. In position 20 asparagine (.alpha.I) is substituted for histidine (.alpha.II). There are 3 amino acid replacements between the .alpha.I-chain in wild ass and in .alpha.-chain in horse (.alpha.24 Phe, .alpha.60 Lys); .alpha.I20 Asn .fwdarw. His, .alpha.23 Asp .fwdarw. Glu, .alpha.131 Thr .fwdarw. Ser. Two amino acid substitutions were found between the .alpha.-chains in zebra and horse, .alpha.20 Asn .fwdarw. His and .alpha.131 Thr .fwdarw. Ser. The .beta.-chains of wild ass and zebra Hb are identical, but 2 amino acid differences were found between wild ass and horse globins, .beta.52 Ala .fwdarw. Gly and .beta.87 Gln .fwdarw. Ala.