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Haemoglobin α Chain Duplication in Barbary Sheep, Ammotragus lervia, Pallas, 1777

Abstract

EVIDENCE for the existence of two non-allelic Hba structural loci in the domestic goat has been presented1,2. The products of these loci, termed Iα and IIα chains3, differ in at least four positions. Glycine, alanine, leucine and asparagine occupy positions 19, 26, 113 and 115 in the Iα chain, respectively, whereas serine, threonine, histidine and serine are present in these positions of the IIα chain2. The percentages of Iα and IIα chains in red cell haemolysates of normal AA goats are about 72 and 28, indicating that evolution of the duplicated Hba loci is associated with a three-fold decrease (or increase) in Hba locus efficiency3. No such α chain multiplicity was observed in the domestic sheep4.

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WILSON, J., WRIGHTSTONE, R. & HUISMAN, T. Haemoglobin α Chain Duplication in Barbary Sheep, Ammotragus lervia, Pallas, 1777. Nature 226, 354–355 (1970). https://doi.org/10.1038/226354a0

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