Primary structure of alpha-globin chains from river buffalo (Bubalus bubalis L.) hemoglobins

Primary structure analysis of the four river buffalo alpha -globin chains s howed that haplotypes A and B differ from each other by a substitution at c odon 64 that may encode Ala or Asn. The A haplotype encodes two a-globin ch ains, (I)alpha1 and (II)alpha3, which differ at positions 129 and 131: (I)a lpha1 has 64 Ala, 129 Phe, 131 Asn; (II)alpha3 has 64 Ala, 129 Leu, 131 Ser . The B haplotype encodes two alpha -globin chains, (I)alpha2 and (II)alpha 4, which differ at positions 10 and 11: (I)alpha2 has 10 Ile, 11 Gln, 64 As n; (II)alpha4 has 10 Val, 11 Lys, 64 Asn. Apart from the Ala/Asn polymorphi sm at position 64, amino acid substitutions in allelic and nonallelic alpha -globin chains seem to have arisen by single point mutations. Detection of electrophoretically silent mutations due to neutral amino acid substitutio ns and their influence on the isoelectric point are discussed. Furthermore, primary structures of river buffalo alpha -globin chains are compared to o ther species of the Bovidae family to suggest evolutionary events that have characterized the amino acid substitutions of river buffalo hemoglobin.