Bhown A S, Bennett J C, Hunter E
J Biol Chem. 1980 Jul 25;255(14):6962-5.
The major internal structural polypeptide (p27) of Rous sarcoma virus (RSV), and the analogous polypeptide (P27(0)) OF Rous-associated virus-O (RAV-O), an endogenous virus released spontaneously by some chicken cells) have been cleaved selectively at a single aspartylprolyl peptide bond to yield two fragments. The NH2- and COOH-terminal amino acid sequences of p27 and p27(0) and their mild acid-cleavage fragments have been determined. These results show the existence of an identical cleavage site and a similar NH2- and COOH-terminal amino acid sequence in both the polypeptides. Furthermore they indicate that the difference in the molecular weights of p27 and p27(0) results from an insertion of amino acids in the COOH-terminal peptide of p27(0) rather than a shift in the scission site of the precursor molecule.
劳氏肉瘤病毒（RSV）的主要内部结构多肽（p27），以及劳氏相关病毒O（RAV - O，一种由某些鸡细胞自发释放的内源性病毒）的类似多肽（P27(0)），已在单个天冬氨酰 - 脯氨酰肽键处被选择性切割，产生两个片段。已确定了p27和P27(0)及其温和酸裂解片段的氨基末端和羧基末端氨基酸序列。这些结果表明，两种多肽中存在相同的切割位点以及相似的氨基末端和羧基末端氨基酸序列。此外，它们表明p27和P27(0)分子量的差异是由于P27(0)的羧基末端肽中插入了氨基酸，而不是前体分子切割位点的偏移。
