Sukhomlinov B F, Datskiv M Z, Maleeva I I
Zh Evol Biokhim Fiziol. 1977 Mar-Apr;13(2):157-61.
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.
通过葡聚糖凝胶过滤（G - 75）从驼鹿、驯鹿和马鹿的肌肉中分离出肌红蛋白制剂。发现它们的铁含量等于0.303 - 0.308%，这相当于分子量为18,000。结果表明，血红素与珠蛋白分离会导致分子在相边界处占据的面积从36×10²增加到47×10² Ų。通过胰蛋白酶水解产物的肽图方法结合肽中单个氨基酸残基的检测，发现所研究的肌红蛋白一级结构有很强的相似性。然而，也获得了表明所研究动物中这种呼吸蛋白具有物种特异性的数据。
