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Amino acid compositions of the tryptic peptides comprising the beta-hemoglobin chain of Macaca nemestrina.

The tryptic peptides comprising the aminoethylated β-hemoglobin chain of Macaca nemestrina were isolated by paper electrophoresis and chromatography. The results of stains for specific amino acids, comparison of peptide maps with those produced by aminoethlated β chains from human hemoglobin A, and amino acid analyses of all peptides in the macaque β chain support the conclusion that the primary structure of the β chain of M. nemestrina is identical to that of the corresponding chains of M. fuscata fuscata and M. fascicularis. The apparent evolutionary conservatism of macaque β chains is discussed in relation to the wide degree of structural variation previously observed among the α-hemoglobin chains of several species of Macaca.