Yoshinaka Y, Luftig R B
J Gen Virol. 1978 Jul;40(1):151-60. doi: 10.1099/0022-1317-40-1-151.
When the partially purified P65-70 proteolytic factor was added at increasing concentrations to 'immature' core sub-particles of Rauscher leukaemia virus (RLV), we observed an increased cleavage of P65-70 (the gag gene product) and P40 (an intermediate cleavage product containing p30) to p30, the major group specific antigen. When examined by electron microscopy the immature cores exhibited a linear decrease in number, with a concomitant increase in the number of mature cores after treatment. Various intermediate structures retaining elements of both immature and mature forms were also observed, suggesting that the in vitro conversion from immature cores to mature cores can occur on a I:I basis.
当将部分纯化的P65 - 70蛋白水解因子以递增浓度添加到劳斯氏白血病病毒(RLV)的“未成熟”核心亚颗粒中时,我们观察到P65 - 70(gag基因产物)和P40(一种含p30的中间裂解产物)裂解为主要群特异性抗原p30的程度增加。通过电子显微镜检查时,未成熟核心的数量呈线性减少,处理后成熟核心的数量随之增加。还观察到了保留未成熟和成熟形式元素的各种中间结构,这表明体外从未成熟核心到成熟核心的转化可以以1:1的比例发生。