Complete Primary Structure of the 3 Chain From the Hemoglobin of a Baboon, Papio cynocephalus

Abstract

The complete primary structure of the β chain from the adult hemoglobin of a baboon, Papio cynocephalus, has been determined by automated, Edman degradation of the intact chain and four fragments derived there from by specific cleavage reactions. The analysis was facilitated by application of a modified solvent system that permits unambiguous identification, by high-performance liquid chromatography, of the 17 amino acids whose phenylthiohydantoin derivatives are soluble in ethyl acetate. The sequence obtained differs from that of the human β chain at eight sites, a degree of divergence similar to that observed when human and macaque β chains are compared. Of the cercopithecoid β chains whose complete sequences have been determined or inferred from compositions of small peptides, that of P. cynocephalus is most like the β chain of the gelada baboon, an observation in accord with assessment of a close phylogenetic relationship between the genera Papio and Theropithecus.