Hebeler B H, Young F E
J Bacteriol. 1976 Jun;126(3):1186-93. doi: 10.1128/jb.126.3.1186-1193.1976.
The major autolysin(s) of Neisseria gonorrhoeae was solubilized from envelopes by extraction with 2% Triton X-100 containing 0.5 M NaCl. Neither Triton X-100 nor NaCl alone could effectively release the autolysin(s). The major autolysin is N-acetylmuramyl-L-alanine amidase (EC 3.5.1.28). The pH optimum for this reaction was broad, ranging from 5.5 to 8.5. Optimal hydrolysis of peptidoglycan occurred in 2% Triton X-100 in 0.1 M KCl. Attempts to purify the autolysin were unsuccessful. A rapid assay for enzyme activity was developed using radioactive cell walls as a substrate ([3H]diaminopimelic acid).
通过用含有0.5M氯化钠的2% Triton X-100提取，从淋病奈瑟菌的包膜中溶解出主要的自溶素。单独的Triton X-100或氯化钠都不能有效地释放出自溶素。主要的自溶素是N-乙酰胞壁酰-L-丙氨酸酰胺酶（EC 3.5.1.28）。该反应的最适pH范围较宽，为5.5至8.5。在0.1M氯化钾的2% Triton X-100中，肽聚糖发生最佳水解。纯化自溶素的尝试未成功。利用放射性细胞壁作为底物（[3H]二氨基庚二酸）开发了一种快速酶活性测定法。
