title: Purification and some properties of two proteases from Pseudomonas aeruginosa No. 700/75.
abstract: Two extracellular proteases have been isolated from the culture supernatant of a virulent strain of Pseudomonas aeruginosa. The enzymes were purified in a three-step procedure involving ammonium sulfate fractionation, acetone precipitation and column chromatography on DE-52 cellulose. The specific activity of protease I was 22.2 U/mg of protein and protease II 6.6 U/mg of protein. Immunological properties and electrophoretic mobilities of the two forms were different. The two forms differ in substrate specificity (only from I exhibited elastinolytic activity) and pH optimum (pH 7.5 and pH 10 for form I and II, respectively).
mesh_terms: D001426:Bacterial Proteins / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D005779:Immunodiffusion; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D011550:Pseudomonas aeruginosa / Q000032:analysis*; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D010447:Peptide Hydrolases