McCalla D R, Reuvers A, Kaiser C
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
J Bacteriol. 1970 Dec;104(3):1126-34. doi: 10.1128/jb.104.3.1126-1134.1970.
When Escherichia coli strain B/r is exposed to 10 to 20 mug of nitrofurazone per ml, mutants with roughly threefold resistance are obtained. Treatment of these mutants with higher concentrations of nitrofurazone yields strains with six- to seven-fold resistance over strain B/r. Each of these steps toward nitrofurazone resistance is accompanied by loss of soluble nitrofurazone reductase activity. When sensitive bacteria are exposed to labeled nitrofurazone or labeled 2-nitrofuran, a considerable amount of radioactivity becomes bound to the cold trichloroacetic acid-insoluble fraction. Very little activity becomes bound in the mutants with six- to seven-fold resistance; mutants with intermediate resistance show intermediate levels of binding. Partially purified nitrofurazone reductase preparations catalyze the conversion of nitrofurazone to compounds which bind to protein and are not removed by prolonged dialysis against 8 m urea or by cold acid. Nitrofurazone reduced by xanthine oxidase or electrolytically reduced also yields compounds which react with protein to form stable derivatives.
当将大肠杆菌B/r菌株暴露于每毫升含10至20微克的呋喃西林时,可获得抗性约为三倍的突变体。用更高浓度的呋喃西林处理这些突变体,可得到比B/r菌株抗性高六至七倍的菌株。这些向呋喃西林抗性发展的每一步都伴随着可溶性呋喃西林还原酶活性的丧失。当敏感细菌暴露于标记的呋喃西林或标记的2-硝基呋喃时,大量放射性物质会与冷的三氯乙酸不溶性部分结合。在抗性为六至七倍的突变体中,结合的活性非常少;具有中等抗性的突变体显示出中等水平的结合。部分纯化的呋喃西林还原酶制剂催化呋喃西林转化为与蛋白质结合且不能通过用8M尿素长时间透析或冷酸去除的化合物。经黄嘌呤氧化酶还原或电解还原的呋喃西林也会产生与蛋白质反应形成稳定衍生物的化合物。