Primate hemoglobins: Their structure, function and evolution—I. Amino acid compositions of the tryptic peptides from the beta chain of Cebus albifrons

Abstract

1. 1. Two fragments were isolated after cyanogen bromide cleavage of the aminoethylated β chain from the major hemoglobin of a New World monkey ( Cebus albifrons). Each fragment was digested with trypsin and the resulting peptides were isolated. The peptides were placed in sequence by homology with the corresponding peptides from the human β chain. The locations of residues that differ from those in the human β chain were deduced from analyses of the thermolysin peptides produced by subfragmentation of selected tryptic peptides. The β chain of C. albifrons differs from that of man at a minimum of seven positions; in addition, two residues (threonine and alanine) were found at position 13. 2. 2. Comparison with β chains from other New World monkeys, Old World monkeys and apes indicates that the ceboid β chains comprise a related group of polypeptide chains which are more similar to those of cercopithecoids than they are to those of hominoids.