The extracellular metalloprotease of Serratia marcescens: I. Purification and characterization.
An extracellular protease of Serratia marcescens produced during growth on skim milk medium was isolated by ethanol precipitation. The protease was purified by salt fractionation, DEAE-cellulose ion exchange chromatography and gel filtration chromatography on Agarose P-100. It has a broad optimum from pH 6.0 to 9.0 and a temperature optimum of 45 degrees C for proteolytic activity on casein. It was classified as a metallo-protease by virtue of its inactivation by metal-ion chelators and reactivation by ferrous ions. Proteolytic activity was not affected by diiso-propylfluorophosphate, p-chloromercuribenzoate and dithiothreitol.
D001665:Binding Sites; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000494:pharmacology; D007700:Kinetics; D008667:Metalloproteins / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D008722:Methods; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D011480:Protease Inhibitors; D012706:Serratia marcescens / Q000201:enzymology*; D013696:Temperature
D008667:Metalloproteins; D011480:Protease Inhibitors; D004492:Edetic Acid; D007501:Iron; D010447:Peptide Hydrolases