Romero-Herrera A E, Lehmann H, Castillo O
Biochim Biophys Acta. 1976 Feb 20;420(2):387-96. doi: 10.1016/0005-2795(76)90330-5.
To the analysis of three prosimian myoglobins reported previously [1, 2] that of the slow loris (Nycticebus coucang) has been added. A cladogram has been constructed utilising the new information to arrive at a possible ancestral prosimian myoglobin. Within the primates only the four prosimians share residues of threonine at position 34 and of isoleucine at position 142. During tryptic digestion of the loris myoglobin, some hydrolysis was observed at bonds not usually considered to be susceptible to the action of this enzyme: 52 Pro-53 Asp, and 120 Pro-121 Gly.
此前已报道过三种原猴亚目动物的肌红蛋白分析结果[1, 2]，现又增加了懒猴（蜂猴）的肌红蛋白分析。利用这些新信息构建了一个进化分支图，以得出可能的原猴亚目祖先肌红蛋白。在灵长类动物中，只有这四种原猴亚目动物在第34位有苏氨酸残基，在第142位有异亮氨酸残基。在对懒猴肌红蛋白进行胰蛋白酶消化时，在通常认为不易受该酶作用的肽键处观察到了一些水解现象：52位脯氨酸-53位天冬氨酸肽键以及120位脯氨酸-121位甘氨酸肽键。
