Identification of an elastolytic protease in stationary phase culture filtrates of M. tuberculosis

FEMS Microbiol Lett. 1997 Jun 1;151(1):59-64. doi: 10.1016/s0378-1097(97)00138-9.

Abstract

Culture filtrate from M. tuberculosis grown in Sauton broth was screened at weekly intervals for elastase and caseinase activity. Both activities were detected concomitantly at 4 weeks and had similar inhibitor and pH profiles. Highest activity occurred between pH 6.5 and pH 7.5. Azocaseinase activity was linear with time between 12 and 28 h at 37 degrees C. Enzymatic activity was inhibited by EDTA, EGTA, dithiothreitol, ethylmaleimide, 1,10-phenanthroline, Zincov, N-tosyl-L-phenylalanine chloromethyl ketone, and N-methoxysuccinyl-Ala-Ala-Pro-Val chloromethyl ketone. SDS-PAGE analysis revealed breakdown of casein after incubation with culture filtrate. These results indicate the presence of a calcium-dependent, elastolytic metalloprotease in stationary phase cultures of M. tuberculosis.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Metalloendopeptidases / analysis*
  • Metalloendopeptidases / drug effects
  • Mycobacterium tuberculosis / enzymology*
  • Pancreatic Elastase / analysis*
  • Pancreatic Elastase / drug effects
  • Protease Inhibitors / pharmacology

Substances

  • Protease Inhibitors
  • Pancreatic Elastase
  • Metalloendopeptidases
  • caseinase