Biochemical studies on haemoglobin variants of the irus macaque

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Abstract
Hemolysates from 202 Macaca irus, imported mainly from Thailand and Vietnam, were examined by starch-gel electrophoresis. In addition to the normal hemoglobin, Hb-Am, two major hemoglobin variants designated as Hb-Pmi and Hb-Qmi and two minor components were found. Hb-Pmi, which occurred in 12%of the sample, forms molecular aggregates, especially when released from the red cell. Peptide analysis showed that it differs from Hb-Ami in the absence of peptides (V-TP III and a-Tp IV. Sera from animals with this hemoglobin in their red cells show two heme-positive bands in addition to the usual single hapto-globin band; this pattern can be produced in the sera of some animals which do not possess it, by addition of Hb-Pmi. Hb-Qmi, which occurred in 24%: of the animals, migrates anodally to Hb-Ami at alkaline pH and does not form aggregates. It is found in two ranges of concentration when present with Hb-Ami. It was shown by recombination experiments to have normal [beta]Ami-chains. The sample was polymorphic for a minor component which was shown to have normal [beta]Ami chains. Some animals have two major hemoglobins and also this minor component and therefore possesses three different non-[beta]-chains. It is suggested that the minor component is the product of a mutated duplicate of the [alpha]-locus. The population genetics of these variant hemoglobins and the possible selective role of simian malaria are discussed.