N-Acetyl- -glucosaminidase, -Glucuronidase and Acid Phosphatase in Mycobacterium leprae

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Abstract
N-acetyl-.beta.-glucosaminidase, .beta.-glucuronidase and acid phosphatase activites were detected in cell-free extracts of M. leprae (from armadillo liver). Extracts of bacteria which had been treated with 7-diazonaphthalene-1,3-disulfonic acid to inactivate surface enzymes retained 30-45% of the activity of the glycosidases and 15% of the activity of the acid phosphatase. When intact bacteria were treated with 1 M NaOH, the corresponding activity in the extracts was 4-9% for the glycosidases and 7% for the acid phosphatase. Inhibition studies with lactones and the use of concavanalin A-agarose showed differences between the glycosidases in extracts of M. leprae and those of armadillo liver. Inhibition studies with vanadate using extracts from NaOH-treated bacteria and extracts of armadillo liver showed differences between the acid phosphatases. Enzymes removed from the surface of M. leprae could have been adsorbed to the surface from host tissue (i.e., lysosomal enzymes) or they could have been extracellular enzymes or associated with the bacterial membrane.