[Purification of protease from staphylococcus aureus (author's transl)].
380 (80%) of 475 Staphylococcus aureus cultures isolated from humans, cattle and dogs were proteolytically active either on casein or gelatin or both (table 1). Protease-activity could also be demonstrated in experimental body-cavities of rabbits (fig. 1). The enzyme-activity was estimated with azocasein. Protease from S. aureus, M 135 precipitated from the culture supernatant with ammonium sulfate at 65% saturation (table 2). It was purified by 2 filtrations on Ultrogel AcA 44 (fig. 2,3) and subsequent isoelectric focusing between pH 3.5-7.0 (fig. 4). The purified protease yielded only 1 line in the SDS-polyacrylamidegel-electrophoresis, in the gelatin-polyacrylamidegel-electrophoresis and in the double immuno-diffusion test (fig. 5). Its isoelectric point was at pH 4.6, and its highest proteolytic activity between pH 7.5-8.3. The molecular weight was estimated by SDS-polyacrylamidegel-electrophoresis to be near 29.000. The protease-activity was completely inhibited in the presence of EDTA, partially inhibited by Cu2+ and Zn2+ and increased by Mn2+ (table 3).
D000818:Animals; D002364:Caseins / Q000378:metabolism; D002417:Cattle; D003300:Copper / Q000494:pharmacology; D004285:Dogs; D004492:Edetic Acid / Q000494:pharmacology; D005337:Fibrin / Q000378:metabolism; D005780:Gelatin / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D013211:Staphylococcus aureus / Q000201:enzymology*; D015032:Zinc / Q000494:pharmacology
D002364:Caseins; D003300:Copper; D005780:Gelatin; D005337:Fibrin; D004492:Edetic Acid; D010447:Peptide Hydrolases; D015032:Zinc
Reinigung einer Protease von Staphylococcus aureus.