Purification and Properties of Spore-lytic Enzymes from Clostridium perfringens Type A Spores
نویسندگان
چکیده
منابع مشابه
Spore lytic enzyme released from Clostridium perfringens spores during germination.
The exudate of fully germinated spores of Clostridium perfringens was found to contain a large amount of a spore lytic enzyme which acted directly on alkali-treated spores of the organism to cause germination. Although no detectable amount of the enzyme was found in dormant spores during germination in a KCl medium, the enzyme was produced rapidly and released into the medium. The optimal condi...
متن کاملA gene (sleC) encoding a spore-cortex-lytic enzyme from Clostridium perfringens S40 spores; cloning, sequence analysis and molecular characterization.
Antiserum was raised against a 31 kDa spore-cortex-lytic enzyme, which is released during germination of Clostridium perfringens S40 spores. Western blotting of dormant spore and vegetative cell fractions separated by SDS-PAGE indicated that the 31 kDa enzyme is spore-specific and that the enzyme in the dormant spore exists as a 36 kDa protein which has no cortex-lytic activity. A gene encoding...
متن کاملPurification and biochemical properties of Clostridium perfringens type A enterotoxin.
The sporulation-specific enterotoxin of Clostridium perfringens type A, which is the toxin active in human food poisoning, has been purified from extracts of sporulating cells. Highly purified enterotoxin was obtained by treatment of crude cell extract with ribonuclease for 30 min, followed by sequential chromatography on Sephadex G-100, Cellex T cellulose, and hydroxylapatite. Recovery was 65 ...
متن کاملPurification and general properties of glutamate decarboxylase from Clostridium perfringens.
1. A seven-step procedure for preparing highly purified glutamate decarboxylase from Clostridium perfringens is described. 2. The homogeneity of the pure enzyme was established by sucrose-density-gradient centrifugation and starch-gel electrophoresis. 3. The isoelectric point of the pure enzyme is about pH4.5 and the molecular weight is 290000. 4. The pH optimum for activity is 4.7. The pure en...
متن کاملPurification and properties of alpha-N-acetylgalactosaminidase from Clostridium perfringens.
Exo-alpha-N-acetylgalactosaminidase has been purified 8000-fold from Clostridium perfringens by gel filtration, ion exchange chromatography, isoelectric precipitation, and negative adsorption on human O type erythrocytes. The resulting enzyme is active at physiological pH and temperature. Phenyl glycosides, oligosaccharides, mucins, glycolipids, and cell membranes are substrates for this enzyme...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Microbiology
سال: 1985
ISSN: 1350-0872,1465-2080
DOI: 10.1099/00221287-131-6-1487