Isolation of a plasmid responsible for caseinase activity in Clostridium perfringens ATCC 3626B

Author:

Blaschek H P,Solberg M

Abstract

Clostridium perfringens strain ATCC 3626B was cured of caseinase activity at a high frequency after treatment with acriflavine dye (2.5%) or elevated temperature growth (9.1%). Caseinase-negative isolates retained the larger (9.4 megadaltons) pHB102 cryptic plasmid, but were missing the smaller (2.1 megadaltons) pHB101 plasmid present in the caseinase-positive wild-type strain. Dye-buoyant density-gradient centrifugation at 4 or 15 degrees C revealed that the pHB101 and pHB102 plasmids are temperature labile and easily converted into the nicked non-supercoiled or linear state.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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1. Clostridium;Bacillus subtilis and Other Gram-Positive Bacteria;2014-04-30

2. Lambda Toxin (Clostridium perfringens);Handbook of Proteolytic Enzymes;2013

3. Lambda toxin (Clostridium perfringens);Handbook of Proteolytic Enzymes;2004

4. VIRULENCE GENES OF CLOSTRIDIUM PERFRINGENS;Annual Review of Microbiology;1998-10

5. Lambda-Toxin ofClostridium perfringensActivates the Precursor of Epsilon-Toxin by Releasing Its N- and C-Terminal Peptides;Microbiology and Immunology;1997-07

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