f Partial characterization of a major autolysin from Mycobacterium phlei
- Authors: Zusheng S. Li†, Terry J. Beveridge, Joanna Betts, Anthony J. Clarke
- Author for correspondence: Anthony J. Clarke. Tel: +1 519 824 4120 ext. 3361. Fax: +1 519 837 1802. e-mail: email@example.com
- Microbiology, January 1999 145: 169-176, doi: 10.1099/13500872-145-1-169
- Subject: Biochemistry
- Published Online:
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.
The SWISS-PROT accession number for the Mycobacterium phlei autolysin reported in this paper is P81528.
Present address: Department of Microbiology and Immunology, Temple University School of Medicine, 3400 North Broad Street, Philadelphia, PA 19140, USA.
© Society for General Microbiology 1999 | Published by the Society for General Microbiology
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