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The extracellular metalloprotease of Serratia marcescens: I. Purification and characterization.

Authors
  • Aiyappa, P S
  • Harris, J O
Type
Published Article
Journal
Molecular and cellular biochemistry
Publication Date
Nov 30, 1976
Volume
13
Issue
2
Pages
95–100
Identifiers
PMID: 12465
Source
Medline
License
Unknown

Abstract

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.

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