Li X M, Trinh K Y, Hew C L, Buettner B, Baenziger J, Davies P L
J Biol Chem. 1985 Oct 25;260(24):12904-9.
Serum antifreeze polypeptides (AFP) from Newfoundland ocean pout have been resolved by ion exchange chromatography and reverse phase high performance liquid chromatography into at least 12 components. The protein sequences of three of the AFP were determined using a combination of protein Edman degradation and cDNA sequencing. The AFP precursor protein encodes for a preprotein of 87 amino acids with no obvious prosequences. Two of the AFP (SP1-A and SP1-C) were separate gene products with minor amino acid sequence differences. The protein structure of SP1-C precursor is MKSVILTGLLFVLLCVDHMTASQSVVAT QLIPINTALTPAMMEGKVTNPIGIPFAEMSQIVGKQVNTPVAKGQTLMPNMVKTYVAGK. The third AFP (SP1-B) is a post-translation modification product of SP1-C. These experiments indicate that the ocean pout AFP are a multigene family with protein structure different from any other known polypeptide antifreezes.
来自纽芬兰海七鳃鳗的血清抗冻多肽（AFP）已通过离子交换色谱法和反相高效液相色谱法分离为至少12种组分。使用蛋白质埃德曼降解法和cDNA测序相结合的方法测定了其中三种AFP的蛋白质序列。AFP前体蛋白编码一个由87个氨基酸组成的前蛋白，没有明显的前导序列。其中两种AFP（SP1-A和SP1-C）是不同的基因产物，氨基酸序列差异较小。SP1-C前体的蛋白质结构为MKSVILTGLLFVLLCVDHMTASQSVVAT QLIPINTALTPAMMEGKVTNPIGIPFAEMSQIVGKQVNTPVAKGQTLMPNMVKTYVAGK。第三种AFP（SP1-B）是SP1-C的翻译后修饰产物。这些实验表明，海七鳃鳗AFP是一个多基因家族，其蛋白质结构不同于任何其他已知的多肽抗冻剂。
