Dene H, Sazy J, Romero-Herrera A E
Biochim Biophys Acta. 1980 Sep 23;625(1):133-45. doi: 10.1016/0005-2795(80)90116-6.
The amino acid sequences of skeletal muscle myoglobins from two old-world monkeys, Presbytis entellus and Erythrocebus patas, as well as one new-world monkey, Cebus apella wer inferred by homology of the tryptic and peptic peptides with the known sequence of human myoglobin and by selective dansyl-Edman degradation. These new sequences were examined phylogentically in conjunction with the 15 primate sequences already reported. It is clear that myoglobin evolution has been extremely conservative among cercopithecoid primates, so much so that the two surviving subfamilies cannot be distinguished using this protein.
通过胰蛋白酶和胃蛋白酶肽段与已知人类肌红蛋白序列的同源性以及选择性丹磺酰-埃德曼降解法，推断出两种旧世界猴（叶猴和赤猴）以及一种新世界猴（僧帽猴）骨骼肌肌红蛋白的氨基酸序列。这些新序列与已报道的15种灵长类序列一起进行了系统发育分析。很明显，在猕猴类灵长类动物中，肌红蛋白的进化极其保守，以至于无法用这种蛋白质区分现存的两个亚科。
