Protease activities during the course of sporulation on Bacillus subtilis.
Three proteolytic enzymes have been isolated from sporulating cultures of Bacillus subtilis. These activities were, respectively, a protease inhibited by ethylenediaminetetraacetic acid (EDTA) but not phenylmethylsulfonyl fluoride (PMSF), a protease active on both protein and ester substrates, and an ester-active enzyme with low activity on proteins. The latter two enzymes were inhibited by PMSF but not by EDTA. The specific activity of each was determined both intra- and extra-cellularly during growth and sporulation in a single-defined medium. All three enzymes were shown to exhibit a rapid increase in specific activity at a time coinciding with the appearance of refractile bodies in cells.
D000645:Ammonium Sulfate; D001412:Bacillus subtilis / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D002474:Cell-Free System; D011232:Chemical Precipitation; D002845:Chromatography; D003470:Culture Media; D003545:Cysteine / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D005459:Fluorides / Q000494:pharmacology; D006358:Hot Temperature; D006882:Hydroxyapatites; D009154:Mutation; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011480:Protease Inhibitors; D011506:Proteins / Q000378:metabolism; D013053:Spectrophotometry; D013170:Spores / Q000254:growth & development*; D013171:Spores, Bacterial / Q000254:growth & development; D013451:Sulfonic Acids / Q000494:pharmacology; D014161:Transduction, Genetic
D003470:Culture Media; D006882:Hydroxyapatites; D011480:Protease Inhibitors; D011506:Proteins; D013451:Sulfonic Acids; D004492:Edetic Acid; D010447:Peptide Hydrolases; D003545:Cysteine; D005459:Fluorides; D000645:Ammonium Sulfate