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The hemoglobins from an asiatic wild ass (Equus hemionus kulan) and a mountain zebra (Equus zebra) were analysed and the complete primary structure of the alpha and beta chains are described. The wild ass globin was separated in two alpha chains (alpha I and alpha II) and one beta-chain by means of chromatography on CM-cellulose in 8M urea buffer at pH 6.5. The wild ass globin shows polymorphism in the alpha-chain like the horse hemoglobin. Under the same chromatographic conditions only one alpha and one beta-chain were found in the zebra globin. The primary structures were determined with the aid of an automatic liquid phase sequenator. A comparison of the sequence data shows there is only one amino acid differing between the alpha I- and alpha II-chain of wild ass. In position 20 asparagine (apha I) is substituted for histidine (alpha II). There are three amino acid replacements between the alpha I-chain in wild ass and an alpha-chain in horse (alpha 24 Phe, alpha 60 Lys); alpha I20 Asn leads to His, alpha 23 Asp leads to Glu, alpha 131 Thr leads to Ser. Two amino acid substitutions were found between the alpha-chains in zebra and horse, alpha 20 Asn leads to His and alpha 131 Thr leads to Ser. The beta-chains of wild ass zebra hemoglobins are identical, but two amino acid differences were found between wild ass and horse globins, beta 52 Ala leads to Gly and beta 87 Gln leads to Ala.

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