Wayne L G, Diaz G A
Tuberculosis Research Laboratory, Veterans Administration Medical Center, Long Beach, California 90822.
J Clin Microbiol. 1987 Sep;25(9):1687-90. doi: 10.1128/jcm.25.9.1687-1690.1987.
The heat-labile T class of mycobacterial catalase exhibits peroxidase activity with some substrates. Most species of mycobacteria produce T-catalase, which is serologically characterized by a combination of shared epitopes and unique, species-specific epitopes. Antibodies to T-catalases from Mycobacterium tuberculosis, Mycobacterium avium, and Mycobacterium intracellulare have been cross absorbed with T-catalases from heterologous species and applied as dots to nitrocellulose membranes. When these membranes were incubated with crude sonic extracts of 93 strains of mycobacteria that produce sufficient T-catalase, and were then exposed to 3,3'-diaminobenzidine peroxidase substrate, only those extracts made from one of the three species represented yielded a discrete brown dot at the site of the corresponding globulin. The sensitivity of the test was at least 96.5%, and the specificity was in excess of 99.5%.
分枝杆菌过氧化氢酶的热不稳定T类对某些底物具有过氧化物酶活性。大多数分枝杆菌菌种都会产生T-过氧化氢酶，其血清学特征是具有共同表位和独特的、菌种特异性表位的组合。针对结核分枝杆菌、鸟分枝杆菌和胞内分枝杆菌的T-过氧化氢酶的抗体已用来自异源菌种的T-过氧化氢酶进行交叉吸收，并作为点样应用于硝酸纤维素膜。当这些膜与93株产生足够T-过氧化氢酶的分枝杆菌的粗超声提取物一起孵育，然后暴露于3,3'-二氨基联苯胺过氧化物酶底物时，只有来自所代表的三种菌种之一的提取物在相应球蛋白的位置产生一个离散的棕色斑点。该试验的灵敏度至少为96.5%，特异性超过99.5%。
