Dene H, Sazy J, Goodman M, Romero-Herrera A E
Biochim Biophys Acta. 1980 Aug 21;624(2):397-408. doi: 10.1016/0005-2795(80)90081-1.
The amino acid sequence of myoglobin from cardiac muscle of the American alligator (Alligator mississippiensis) was established by alignment of overlapping peptides and dansyl-Edman degradation. The chain initiating methonine seems to be retained. Thus, this molecule has 154 amino acid residues rather than 153 as in other tetrapod myoglobins. Maximum parsimony analysis indicated that alligator myoglobin diverges more from both bird and mammal myoglobins than these latter do from each other. The phylogenetic implications are discussed with respect to a possible diphyletic origin for diapsid reptiles.
通过重叠肽段比对和丹磺酰-埃德曼降解法确定了美国短吻鳄（密西西比鳄）心肌肌红蛋白的氨基酸序列。起始甲硫氨酸残基似乎得以保留。因此，该分子有154个氨基酸残基，而非其他四足动物肌红蛋白中的153个。最大简约法分析表明，短吻鳄肌红蛋白与鸟类和哺乳动物肌红蛋白的差异，比鸟类和哺乳动物肌红蛋白之间的差异更大。文中还就双孔亚纲爬行动物可能的双源起源探讨了系统发育学意义。
