Complete Sequence of the γ Chain from the Fetal Hemoglobin of the Baboon, Papio cynocephalus

Abstract

The amino acid sequence of the hemoglobin γ chain from a baboon, Papio cynocephalus, was determined by automated sequencing of the intact chain and six fragments generated by specific cleavage reactions. the existence of structural heterogeneity at position 75, where both valyl and isoleucyl residues were found, is suggestive of the presence of nonallelic ^Vγ and ^Iγ-chain genes in this species, and further emphasizes the extent to which the genetic basis of hemoglobin production among many higher primates is similar. Comparison of the sequences of those γ chains from Homo sapiens, Pan troglodytes, Macaca nemestrina and P. cynocephalus that have been well characterized attests to the conservative nature of γ-chain evolution among the Anthropoidea, the differences in sequence between any two of these chains ranging from none (between the Aγ and Gγ chains of P. troglodytes and H. sapiens) to no more than five (between the _Vγ chains of p. cynocephalus and the ^Aγ chains of H. sapiens).