PMID: 37166May 1, 1979

Purification and characterization of a Serratia marcescens metalloprotease

Infection and Immunity
D Lyerly, A Kreger


An extracellular, nonelastolytic, neutral metalloprotease of Serratia marcescens was purified by sequential ammonium sulfate precipitation, hydroxyapatite adsorption chromatography, flat-bed isoelectric focusing, and Sephadex G-100 gel filtration. The protease preparation had a 280/260 nm absorbance ratio of 1.8, was free of detectable amounts of endotoxin, carbohydrate, phosphorus, and other known extracellular enzymes of S. marcescens, and was homogeneous by Ouchterlony double immunodiffusion and Grabar-Williams immunoelectrophoresis. Crossed immunoelectrophoresis, thin-layer electrofocusing in polyacrylamide gel, and polyacrylamide disc gel electrophoresis showed three to four closely migrating, Coomassie blue-staining components in the protease preparation. However, zymogram analyses of the patterns showed that protease activity was associated with each component and that the protease was, therefore, microheterogeneous. The isoelectric point and sedimentation coefficient of the protease were approximately 5.3 to 5.4 and 4.2S, respectively, and the molecular weight estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by gel filtration was approximately 52,500 and 44,000, respectively. The pH optimum ran...Continue Reading


Aug 5, 2003·Canadian Journal of Microbiology·Katsuji WatanabeKoichi Hayano
Jan 1, 1987·Microbiology and Immunology·N MiyoshiS Shinoda
Feb 1, 1987·Acta Ophthalmologica·E M SalonenA Vaheri
Feb 1, 1986·The Journal of Dairy Research·D J Fairbairn, B A Law

Related Concepts

Serratia marcescens
Extracellular Space
Peptide Hydrolases
Hydrogen-Ion Concentration
Protease Inhibitors

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