García P, García E, Ronda C, Lopez R, Jiang R Z, Tomasz A
J Gen Microbiol. 1986 May;132(5):1401-5. doi: 10.1099/00221287-132-5-1401.
Two mutants of Streptococcus pneumoniae deficient in autolysin activity produced a protein that showed immunological identity with the N-acetyl-muramyl-L-alanyl-amidase present in the wild-type strain, when tested with antiserum obtained against this enzyme. The protein was produced by the mutant cultures grown either at 37 degrees C or at 30 degrees C, although only the cell extracts obtained at 30 degrees C showed significant cell wall hydrolysing activity. In contrast to the lysis resistance of these bacteria grown at 37 degrees C, mutant cultures grown at 30 degrees C exhibited significant degrees of autolysis when treated with detergent or cell wall inhibitors. Extracts of the mutant cultures contained a cell wall hydrolysing activity that was rapidly inactivated during incubation at 37 degrees C.
两种自溶素活性缺陷的肺炎链球菌突变体产生了一种蛋白质,当用针对该酶获得的抗血清进行检测时,该蛋白质与野生型菌株中存在的N-乙酰胞壁酰-L-丙氨酰胺酶表现出免疫同一性。该蛋白质由在37℃或30℃下生长的突变体培养物产生,尽管只有在30℃下获得的细胞提取物显示出显著的细胞壁水解活性。与在37℃下生长的这些细菌的裂解抗性相反,在30℃下生长的突变体培养物在用去污剂或细胞壁抑制剂处理时表现出显著程度的自溶。突变体培养物的提取物含有一种细胞壁水解活性,该活性在37℃孵育期间迅速失活。