[Comparative study of the myoglobin of the reindeer Rangifer tarandus, the elk Alces alces and the deer Cervus elaphus xanthopygus].

Myoglobin preparations from muscles of A. alces, R. tarandus and C. elaphus xanthopygus were isolated by Sephadex gel filtration (G-75). Their Fe content was found to be equal to 0.303--0.308%, which corresponds to the molecular weight of 18, 000. It was shown that splitting of heme from the globin results in an increase of the area occupied by the molecule on the phase boarderline from 36-10(2) to 47-10(2) A2. By the peptide charts method of tryptic hydrolysates combined with the detection of separate amino acid residues in peptides, strong similarities in the primary structure of the myoglobins investigated were found. However, data were obtained which indicate species specificity of this respiratory protein in the animals studied.