Yoshinaka Y, Luftig R B
J Gen Virol. 1981 May;54(Pt 1):33-8. doi: 10.1099/0022-1317-54-1-33.
Although the Pr65gag precursor polyproteins of Moloney murine leukaemia virus (M-MuLV) and of Rauscher murine leukaemia virus (R-MuLV) have the same apparent mol. wt. by SDS--polyacrylamide gel electrophoresis (SDS--PAGE), their initial approximately 40 000 dalton intermediate cleavage products differ in mol. wt., i.e. the M-MuLV product (Pr41.5gag) is 1500 daltons larger than the R-MuLV product (Pr40gag). We took advantage of this difference to show that in vitro cleavage of R-MuLV Pr65gag by the M-MuLV proteolytic activity gives rise to R-MuLV Pr40gag and not M-MuLV Pr41.5gag. This result suggests that the specificity for cleavage of the MuLV Pr65gag is built into the substrate.
尽管莫洛尼鼠白血病病毒(M-MuLV)和劳舍尔鼠白血病病毒(R-MuLV)的Pr65gag前体多聚蛋白经十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)测定具有相同的表观分子量,但它们最初约40000道尔顿的中间裂解产物分子量不同,即M-MuLV产物(Pr41.5gag)比R-MuLV产物(Pr40gag)大1500道尔顿。我们利用这一差异表明,M-MuLV的蛋白水解活性在体外对R-MuLV Pr65gag的裂解产生的是R-MuLV Pr40gag而非M-MuLV Pr41.5gag。这一结果表明,MuLV Pr65gag的裂解特异性存在于底物中。