Gleisner J M, Ramthun C A
Microbios. 1981;32(127):15-27.
The aminopeptidase activity of three strains of Mycobacterium tuberculosis, H37Rv, H37Ra, and M. tuberculosis from a patient, was partially purified and characterized. The activity from all three organisms was found to be very similar, if not identical. All three aminopeptidases eluted at a similar salt concentration on DEAE Bio-Gel; were active on the same synthetic and peptide substrates; had molecular weights of 75-76,000; were found to be stable between pH 5 and 8, and 4 degrees and 40 degrees C; and had a pH optimum of 7. They were inhibited by low concentrations of Hg2+, Cu2+ and Co2+; metal chelators; and 4-chloromercuribenzoic acid. A number of amino acids and several antibiotics were also found to be inhibitory. Of the antibiotics tested, rifampicin and bacitracin were the most effective.
对来自一名患者的三株结核分枝杆菌（H37Rv、H37Ra和结核分枝杆菌）的氨肽酶活性进行了部分纯化和特性鉴定。发现来自所有三种菌株的活性即便不完全相同也非常相似。所有三种氨肽酶在DEAE生物凝胶上以相似的盐浓度洗脱；对相同的合成底物和肽底物有活性；分子量为75 - 76,000；发现在pH 5至8以及4℃至40℃之间稳定；最适pH为7。它们受到低浓度的Hg2 +、Cu2 +和Co2 +、金属螯合剂以及4 - 氯汞苯甲酸的抑制。还发现一些氨基酸和几种抗生素具有抑制作用。在所测试的抗生素中，利福平和杆菌肽最为有效。
