Schrag J D, Cheng C H, Panico M, Morris H R, DeVries A L
Department of Physiology and Biophysics, University of Illinois, Urbana.
Biochim Biophys Acta. 1987 Oct 15;915(3):357-70. doi: 10.1016/0167-4838(87)90021-5.
Antifreeze peptides were isolated from Rhigophila dearborni, an antarctic eel pout, and Lycodes polaris, an arctic eel pout (both from the family Zoarcidae). The primary structures of two peptides, one from each species, were determined using a combination of Edman degradation and mass spectrometric techniques. The two sequences show a high degree of homology with nearly 80% of the residues being identical. These peptides are also homologous to antifreeze peptides from a third eel pout which inhabits the north Atlantic Ocean. The CD spectra of all of these peptides are also very similar. Unlike the antifreeze peptides of cottid fishes, the structures of antifreeze peptides from zoarcid fishes appear to be highly conserved, despite the large geographic distances which separate the different species. The zoarcid peptides also appear to have structures very different from other fish antifreezes.
抗冻肽是从南极粘鱼(Rhigophila dearborni)和北极粘鱼(Lycodes polaris,均属于绵鳚科)中分离出来的。利用埃德曼降解法和质谱技术相结合的方法,确定了来自这两个物种各一种肽的一级结构。这两个序列显示出高度的同源性,近80%的残基相同。这些肽也与栖息在北大西洋的第三种粘鱼的抗冻肽同源。所有这些肽的圆二色光谱也非常相似。与杜父鱼的抗冻肽不同,尽管不同物种之间地理距离遥远,但绵鳚科鱼类的抗冻肽结构似乎高度保守。绵鳚科肽的结构也似乎与其他鱼类抗冻蛋白非常不同。