Villanueva N, Lázaro J M, Salas M
Eur J Biochem. 1981 Jul;117(3):499-505. doi: 10.1111/j.1432-1033.1981.tb06365.x.
The purification of the neck appendage protein of phi 29, p12*, which is involved in the adsorption of the phage to Bacillus subtilis, is described. The purified native protein is in a dimeric form and can be assembled, in vitro, onto purified 12- particles that lack the neck appendages, suggesting that the incorporation of p12* to the rest of the phage structure is a self-assembly process. The assembly of protein p12* in vitro follows cooperative kinetics and it occurs with an efficiency of about 4%.
本文描述了与噬菌体φ29吸附枯草芽孢杆菌相关的颈部附属蛋白p12的纯化过程。纯化后的天然蛋白呈二聚体形式，并且能够在体外组装到缺乏颈部附属结构的纯化12 - 颗粒上，这表明p12整合到噬菌体结构的其余部分是一个自组装过程。蛋白p12*在体外的组装遵循协同动力学，其组装效率约为4%。
