title: Purification and properties of spore-lytic enzymes from Clostridium perfringens type A spores.
abstract: Spores of Clostridium perfringens contain at least two spore-lytic enzymes active in hydrolysing cortical peptidoglycan. One enzyme has been purified 1800-fold and has a molecular weight of 17 400 determined from chromatography on Sephadex G-75. Two protein bands were apparent after SDS-PAGE. The isolated enzyme was investigated for response to temperature, pH, ionic strength and enzyme inhibitors, and for mode of action. A second enzyme activity, differing from the first in apparent molecular weight (29 800) as determined by gel exclusion chromatography, and also in its pH optimum and activity on cortical substrate, was also isolated, although not purified to the same extent.
authors.forename: D E
authors.initials: DE
authors.lastname: Gombas
authors.forename: R G
authors.initials: RG
authors.lastname: Labbe
mesh_terms: D002850:Chromatography, Gel; D003016:Clostridium perfringens / Q000201:enzymology / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000302:isolation & purification*; D008970:Molecular Weight; D013171:Spores, Bacterial / Q000201:enzymology; D013696:Temperature
chemical_list: D006867:Hydrolases