Fetal hemoglobin of the rhesus monkey, Macaca mulatta: complete primary structure of the .gamma. chain

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Abstract
The complete amino acid sequence of the .gamma. chain from the major 1 of 2 fetal Hb from the rhesus monkey, M. mulatta, was determined by automated, stepwise degradation of selected fragments produced by cleavage at methionyl and tryptophanyl residues and at the single aspartylprolyl bond. The minor fetal Hb is similar to human Hb F1 in relative electrophoretic and chromatographic properties and in the level at which it is found (about 12% of the total Hb F). Apparently this minor component contains, like Hb F1, .gamma. chains that differ from those of the major component by virtue of acetylation of their amino-terminal glycyl residues. Although the .gamma. chains of most anthropoid primates are structurally heterogeneous and appear to be encoded by nonallelic genes, no sign of structural heterogeneity was detected at any position in the major .gamma. chain from M. mulatta. If nonallelic .gamma.-chain genes exist in this species, the chains encoded by them may be identical in sequence. The .gamma. chain from M. mulatta is but the 6th primate .gamma. chain whose primary structure was fully characterized. The slight extent of structural divergence among these chains (the 4 chains from various species of Old World monkeys differ from one another by no more than 2 substitutions, while the human and cercopithecoid .gamma. chains differ at no more than 5 sites) attests to the conservative nature of .gamma.-chain evolution among the higher primates.