Hengstenberg W, Penberthy W K, Hill K L, Morse M L
J Bacteriol. 1969 Aug;99(2):383-8. doi: 10.1128/jb.99.2.383-388.1969.
The phosphotransferase system of Staphylococcus aureus was characterized. Mutants defective in enzyme I and heat-stable (HPr) protein as well as in the two components specific to lactose accumulation, factor III and enzyme II, were isolated. Colorimetric assays for each of the components are presented based on the formation of o-nitrophenyl-beta-d-galactoside-6-phosphate by the system and its hydrolysis by the staphylococcal 6-phospho-beta-galactosidase. The components were partially purified and their molecular weights were estimated: enzyme I, 100,000 +/- 15%; HPr, 10,000 +/- 15%; factor III, 30,000 +/- 15%; 6-phospho-beta-galactosidase, 45,000. Enzyme II is a membrane-bound protein.
对金黄色葡萄球菌的磷酸转移酶系统进行了表征。分离出了在酶I、热稳定(HPr)蛋白以及乳糖积累特异性的两个组分(因子III和酶II)方面存在缺陷的突变体。基于该系统形成邻硝基苯基-β-D-半乳糖苷-6-磷酸并由葡萄球菌6-磷酸-β-半乳糖苷酶将其水解,给出了各组分的比色测定法。对这些组分进行了部分纯化并估计了它们的分子量:酶I为100,000±15%;HPr为10,000±15%;因子III为30,000±15%;6-磷酸-β-半乳糖苷酶为45,000。酶II是一种膜结合蛋白。