Rousseaux J, Dautrevaux M, Han K
Biochim Biophys Acta. 1976 Jul 19;439(1):55-62. doi: 10.1016/0005-2795(76)90160-4.
The primary structure of pig heart myoglobin has been established by study of the tryptic peptides of whole globin and by analysis of the fragments obtained by CNBr cleavage. Thermolysin and chymotrypsin digestion were used to determine the sequence of the M fragment (56-131). Automatic Edman degradation of whole globin and of the M fragment completed the sequence of pig myoglobin. Comparison with other ungulates shows that pig myoglobin is far from other artiodactyls previously studied (ox and sheep) and close to the eutherian ancestral chain.
通过对完整球蛋白的胰蛋白酶肽段进行研究以及对经溴化氰裂解获得的片段进行分析,已确定猪心脏肌红蛋白的一级结构。利用嗜热菌蛋白酶和胰凝乳蛋白酶消化来确定M片段(56 - 131)的序列。对完整球蛋白和M片段进行自动埃德曼降解,完成了猪肌红蛋白的序列测定。与其他有蹄类动物比较表明,猪肌红蛋白与先前研究过的其他偶蹄目动物(牛和羊)差异较大,而与真兽类祖先链相近。