Amino acid differences between the ?-chains from two hemoglobins of the yellow-cheeked vole (family cricetidae)

Abstract

The yellow-cheeked vole (Microtus xanthognathus) shows two electrophoretic hemoglobin components. Electrophoresis of the polypeptide chains from the separated hemoglobin components shows identical beta-chains but two alpha-chains of different mobility, alphaf and alphas. The composition of soluble tryptic peptides was determined for each alpha-chain. Amino acid differences were found in peptides alpha T1 and alpha T9; the compositions of the remainder of the homologous peptides were identical. Differences in alpha T1, found at alpha4 (alpha2-Gly-alphaf-Val) and alpha 5 (alphas-Thr-alphaf-Asp), were confirmed after a run to residue 20 of the fast component in an automatic sequencer. The differences in charge between alphaT1 peptides can account for the electrophoretic pattern of two hemoglobins. This is the first time that it has been possible to identity the residues which can account for the charge difference between the two hemoglobins observed in a Microtus species.

CLOSELY LINKED ALPHA‐CHAIN HEMOGLOBIN LOCI IN PEROMYSCUS AND OTHER ANIMALS: SPECULATIONS ON THE EVOLUTION OF DUPLICATE LOCI

“…Since there seemed to be no mechanism whereby separate loci could mutate jointly and in exactly the same fashion, Clegg (1974) concluded that achain gene duplications must have occurred recently and independently in those three species of Equus. Duffy et al (1976) reached a similar conclusion from a-globin sequences in the rodent families Muridae and Cricetidae. The minimal divergence between duplicate loci within families, contrasted with marked divergence between families, led Duffy and his colleagues to postulate that a-globin duplications occurred after the divergence of the murid and cricetid stem lines.…”

Relaxed functional constraints on triplicate α-globin gene in the bank vole suggest a different evolutionary history from other rodents

“…Relaxed evolutionary constraints on a rodent a-globin gene S Marková et al example, Ferrand, 1989) and separated them by cellulose acetate membrane electrophoresis with a tris-borate-EDTA buffer (pH 8.9) in 8 M urea (Duffy et al, 1976). The electrophoresis was carried out at 450 V for 105 min at 4 1C.…”