Intracellular proteases during sporulation and enterotoxin formation by Clostridium perfringens type A

Alicia Löffler, Ronald G. Labbe*

*Corresponding author for this work

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Intracellular proteolytic activity was detected in cell-free extracts of Clostridium perfringens NCTC 10239 and NCTC 8798. The kinetics of protease, enterotoxin, and spore formation as well as growth of the wild type at elevated temperature and the use of sporulation mutants indicated that most protease activity was related to sporulation. Intracellular protease activity was inhibited by a mixture of tetrasodium ethylenediaminetetraacetic acid and phenylmethylsulfonyl fluoride; this indicated the presence of an alkaline serine protease and a neutral metallo-protease. Stage 0 sporulation mutants produced only metallo-sensitive proteases; this indicated that only the serine protease was sporulation-specific.

Original languageEnglish (US)
Pages (from-to)187-190
Number of pages4
JournalCurrent Microbiology
Volume8
Issue number3
DOIs
StatePublished - May 1 1983

ASJC Scopus subject areas

  • Microbiology
  • Applied Microbiology and Biotechnology

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