Partial characterization of a major autolysin from Mycobacterium phlei
Li, Zusheng S. and Beveridge, Terry J. and Betts, Joanna and Clarke, Anthony J.,, 145, 169-176 (1999),
doi = https://doi.org/10.1099/13500872-145-1-169,
publicationName = Microbiology Society,
issn = 1350-0872,
abstract= Summary: Autolytic enzyme profiles of fast- and slow-growing mycobacteria were examined using SDS-PAGE zymography with incorportated mycobacterial peptidoglycan sacculi as substrate. Each species tested (Mycobacterium phlei, Mycobacterium smegmatis, Mycobacterium aurum, Mycobacterium fortuitum and Mycobacterium kansasii) appeared to produce a different set of enzymes on the basis of differing number and molecular masses. A major autolysin from M. phlei was purified to apparent homogeneity by DEAE-cellulose chromatography, preparative gel electrophoresis and Mono Q FPLC. This enzyme had an estimated molecular mass of 38 kDa, an isoelectric point of 5·5 and a pH optimum of pH 7·5. Digestion of purified peptidoglycan by the enzyme resulted in the appearance of reducing sugars, suggesting that the 38 kDa autolysin is a β-glycosidase. Partial internal amino acid sequence of the autolysin was determined and should facilitate identification, cloning and overexpression of the encoding gene.,
language=,
type=