Hemoglobins in sheep: multiple differences in amino acid sequences of three beta-chains and possible origins.

Among the three adult sheep hemoglobins (A, B, and C), two (A and B) are reportedly products of alleles. The beta-chains of A and B differ by at least seven scattered amino acid residues whereas the beta-sequence of C differs from A by at least 16 residues and from B by at least 21 residues. These changes suggest that the origin of C-beta antedated the divergence of A and B. Five shared differences between A-beta and C-beta with respect to B-beta can be interpreted as the result of selective advantage in favor of B. A complex of additional mechanisms has possibly been involved in maintaining the A-B- C porymorphism.