Makino S, Woolford J L, Tanford C, Webster R E
J Biol Chem. 1975 Jun 10;250(11):4327-32.
The major coat protein of bacteriophage f1, which is localized in the host membrane during phage maturation, has a hydrophobic binding site capable of binding deoxycholate and a variety of detergents to form a soluble particle, and in that respect, resembles many membrane proteins. The soluble particle has properties that suggest it is formed by simple insertion of protein into a deoxycholate or detergent micelle, but molecular weight measurements show that the protein is present as a dimer, even in sodium dodecyl sulfate, indicating the existence of unusually strong forces for self-association. A by-product of the investigation has been to show that detergents can be very helpful in the fractionation of the constituent molecules of the virus: deoxycholate-solubilized virus is readily fractionated by gel chromatography into DNA, A protein, and B protein, with virtually no cross-contamination.
噬菌体f1的主要外壳蛋白在噬菌体成熟过程中定位于宿主膜上，它有一个疏水结合位点，能够结合脱氧胆酸盐和多种去污剂以形成可溶性颗粒，在这方面，它类似于许多膜蛋白。该可溶性颗粒的特性表明它是由蛋白质简单插入脱氧胆酸盐或去污剂胶束中形成的，但分子量测量表明，即使在十二烷基硫酸钠中，该蛋白质也以二聚体形式存在，这表明存在异常强大的自我缔合作用力。该研究的一个副产品是表明去污剂在病毒组成分子的分级分离中非常有用：脱氧胆酸盐增溶的病毒很容易通过凝胶色谱法分级分离成DNA、A蛋白和B蛋白，几乎没有交叉污染。
