{"title":"组织源性分枝杆菌过氧化氢酶的血清学表征方法。","authors":"V M Katoch, L G Wayne, G A Diaz","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Cell-free extracts of Mycobacterium lepraemurium from mouse liver and M. leprae from armadillo liver were analysed for the presence of any mycobacterial catalase by using the specific inhibitor 3-amino-1,2,4-triazole and seroprecipitation titrations. These studies clearly demonstrated the presence of a \"T\" type of mycobacterial catalase in M. lepraemurium and placed it, in terms of immunological distance, in a position between M. tuberculosis and M. avium. The results did not reveal any detectable \"T\" catalase activity in the M. leprae preparations. The \"M\" type catalase activity which was observed did not bind to antisera against \"M\" catalase of M. kansasii, but was bound to the extent of 80% to antisera against normal armadillo liver catalase. The significance of the component of the \"M\" catalase in M. leprae preparations which did not react against antibodies to normal liver remains to be determined.</p>","PeriodicalId":7904,"journal":{"name":"Annales de microbiologie","volume":"133 3","pages":"407-14"},"PeriodicalIF":0.0000,"publicationDate":"1982-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Serological approaches for the characterization of catalase in tissue-derived mycobacteria.\",\"authors\":\"V M Katoch, L G Wayne, G A Diaz\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Cell-free extracts of Mycobacterium lepraemurium from mouse liver and M. leprae from armadillo liver were analysed for the presence of any mycobacterial catalase by using the specific inhibitor 3-amino-1,2,4-triazole and seroprecipitation titrations. These studies clearly demonstrated the presence of a \\\"T\\\" type of mycobacterial catalase in M. lepraemurium and placed it, in terms of immunological distance, in a position between M. tuberculosis and M. avium. The results did not reveal any detectable \\\"T\\\" catalase activity in the M. leprae preparations. The \\\"M\\\" type catalase activity which was observed did not bind to antisera against \\\"M\\\" catalase of M. kansasii, but was bound to the extent of 80% to antisera against normal armadillo liver catalase. The significance of the component of the \\\"M\\\" catalase in M. leprae preparations which did not react against antibodies to normal liver remains to be determined.</p>\",\"PeriodicalId\":7904,\"journal\":{\"name\":\"Annales de microbiologie\",\"volume\":\"133 3\",\"pages\":\"407-14\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1982-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Annales de microbiologie\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Annales de microbiologie","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Serological approaches for the characterization of catalase in tissue-derived mycobacteria.
Cell-free extracts of Mycobacterium lepraemurium from mouse liver and M. leprae from armadillo liver were analysed for the presence of any mycobacterial catalase by using the specific inhibitor 3-amino-1,2,4-triazole and seroprecipitation titrations. These studies clearly demonstrated the presence of a "T" type of mycobacterial catalase in M. lepraemurium and placed it, in terms of immunological distance, in a position between M. tuberculosis and M. avium. The results did not reveal any detectable "T" catalase activity in the M. leprae preparations. The "M" type catalase activity which was observed did not bind to antisera against "M" catalase of M. kansasii, but was bound to the extent of 80% to antisera against normal armadillo liver catalase. The significance of the component of the "M" catalase in M. leprae preparations which did not react against antibodies to normal liver remains to be determined.