Leonard C G, Cole R M
J Bacteriol. 1972 Apr;110(1):273-80. doi: 10.1128/jb.110.1.273-280.1972.
A procedure for the isolation and purification of competence factor produced in a defined medium by group H streptococci, strain Challis-6, is presented. Partial characterization and chemical analysis of the product are described. The procedure yields competence factor of high purity, as shown by homogeneity in electrofocusing, by electrophoresis in sodium dodecyl sulfate polyacrylamide gels, and by chemical analysis. The data indicate that competence factor is a small, dialyzable, highly basic compound. It is free from lipids, phosphorus, and carbohydrates, and is colorless and thermoresistant. Its biological activity is destroyed by trypsin but not by deoxyribonuclease, ribonuclease, lipase, or lysozyme. Its high isoelectric point of above pH 11.0 suggests that competence factor may be a protamine or a polymer of basic amino acids. The possibility that a polyamine may be an integral part of the polypeptide molecule has not been excluded.
本文介绍了一种从H组链球菌Challis - 6菌株在特定培养基中产生的感受态因子进行分离和纯化的方法。文中描述了该产物的部分特性和化学分析。如通过等电聚焦、十二烷基硫酸钠聚丙烯酰胺凝胶电泳和化学分析显示的均一性所示,该方法可产生高纯度的感受态因子。数据表明感受态因子是一种小分子、可透析、高碱性的化合物。它不含脂质、磷和碳水化合物,无色且耐热。其生物活性可被胰蛋白酶破坏,但不会被脱氧核糖核酸酶、核糖核酸酶、脂肪酶或溶菌酶破坏。其高于pH 11.0的高电泳等点表明感受态因子可能是一种鱼精蛋白或碱性氨基酸聚合物。尚未排除多胺可能是多肽分子组成部分的可能性。