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

The complete amino acid sequence of the gamma chain from the major one of two fetal hemoglobins from the rhesus monkey, Macaca 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 hemoglobin is single aspartylprolyl bond. The minor fetal hemoglobin 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). On these grounds, we assume that this minor component contains, like Hb FI, 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 antropoid primates examined to date are structurally heterogeneous and, hence, 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. Thus, 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 sixth primate gamma chain whose primary structure has been fully characteerized. The slight extent of structural divergence among these chains (the four chains from various species of Old World monkeys differ from one another by no more than two substitutions, while the human and cercopithecoid gamma chains differ at no more than five sites) attests to the conservative nature of gamma-chain evolution among the higher primates.