Goldsmith M E, Konigsberg W H
Biochemistry. 1977 Jun 14;16(12):2686-94. doi: 10.1021/bi00631a016.
The adsorption (minor coat) protein of the bacteriophage fd has been implicated to function in several steps of viral morphogenesis. The protein has been purified by sodium dodecyl sulfate gel filtration after dissociation of the virus. The adsorption protein preparation was estimated to have less than 5% contamination by analysis on sodium dodecyl sulfate-polyacrylamide gels and by the results of semiquantitative dansyl-Edman degradation. The amino-terminal sequence of the adsorption protein is H2N-Ala-Glx-Thr-Val-Glx-Ser-Pro-Leu-Pro-. Carboxypeptidase A plus B digestion of the protein under a variety of denaturing conditions did not release any amino acids. There are 3-4 adsorption proteins per virion as estimated by the distribution of E114C]leucine between the major and minor coat protein peaks on sodium dodecyl sulfate-polyacrylamide gels. Adsorption protein-specific antibodies were induced in the rabbit and used as electronmicroscopic markers to determine the position of the adsorption proteins in the viral particle. The adsorption proteins were found at only one end of the filamentous viral particles.
噬菌体fd的吸附（次要衣壳）蛋白被认为在病毒形态发生的几个步骤中发挥作用。在病毒解离后，通过十二烷基硫酸钠凝胶过滤法对该蛋白进行了纯化。通过十二烷基硫酸钠-聚丙烯酰胺凝胶分析以及半定量丹磺酰-埃德曼降解结果估计，吸附蛋白制剂的污染率低于5%。吸附蛋白的氨基末端序列为H2N-Ala-Glx-Thr-Val-Glx-Ser-Pro-Leu-Pro-。在各种变性条件下，用羧肽酶A和B对该蛋白进行消化，未释放出任何氨基酸。根据[14C]亮氨酸在十二烷基硫酸钠-聚丙烯酰胺凝胶上主要和次要衣壳蛋白峰之间的分布情况估计，每个病毒粒子有3至4个吸附蛋白。在兔子体内诱导产生了吸附蛋白特异性抗体，并将其用作电子显微镜标记物，以确定吸附蛋白在病毒颗粒中的位置。结果发现，吸附蛋白仅存在于丝状病毒颗粒的一端。
