title: Purification and partial characterization of a spore cortex-lytic enzyme of Clostridium perfringens S40 spores.
abstract: A spore cortex-lytic enzyme was purified in an active form from the exudate of fully germinated spores of Clostridium perfringens S40. The enzyme caused attenuation of absorbance in coatless spore suspensions and phase-darkening of the spores, but had minimal activity on isolated peptidoglycan fragments. The enzyme was identified as a 31 kDa protein which is probably an N-acetylmuramyl-L-alanine amidase. The amino-terminal 15 residues of the enzyme were: VLPEPVVPEYIVVHN.
authors.affiliation: Department of Applied Biological Sciences, School of Agricultural Sciences, Nagoya University, Aichi, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Miyata
authors.forename: R
authors.initials: R
authors.lastname: Moriyama
authors.forename: K
authors.initials: K
authors.lastname: Sugimoto
authors.forename: S
authors.initials: S
authors.lastname: Makino
mesh_terms: D000595:Amino Acid Sequence; D003016:Clostridium perfringens / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000737:chemistry / Q000302:isolation & purification*; D011189:Potassium Chloride; D013171:Spores, Bacterial / Q000201:enzymology*; D013696:Temperature
chemical_list: D011189:Potassium Chloride; D009238:N-Acetylmuramoyl-L-alanine Amidase