PMID: 42639Dec 1, 1979

Isolation and properties of the protease from the wild-type and mutant strains of Pseudomonas fragi

Journal of Bacteriology
J Noreau, G R Drapeau

Abstract

A simplified procedure for the purification of the extracellular protease of Pseudomonas fragi was developed. The enzyme was isolated from a derepressed mutant producing 40 times the enzyme level of the parental organism. It was collected from culture filtrates by ammonium sulfate precipitation, and it was obtained in pure form by single chromatography on a column of diethylaminoethyl cellulose. The protease had a molecular weight of 52,000 as estimated by sodium dodecyl sulfate-gel electrophoresis and had properties of a classical neutral endopeptidase with the exception of its substrate specificity. Mutants of P. fragi producing proteases of altered substrate specificities were isolated from plates containing elastin as the sole carbon source. The SP-Sephadex elution patterns of enzymes extracted from each mutant examined were complex, suggesting that either the enzyme was autodigested or several active forms could be generated from a common precursor. The substrate specificities of the mutant enzymes were different from that produced by the parental strain.

References

Jul 1, 1993·International Journal of Peptide and Protein Research·R DharanipragadaV J Hruby
Oct 9, 2002·Proceedings of the National Academy of Sciences of the United States of America·Li NiuH Gobind Khorana
Oct 3, 1998·The Journal of Biological Chemistry·H JungR Schmid
Nov 5, 1999·Molecular Reproduction and Development·F ZhangJ Ausió
Mar 1, 1987·The Journal of Applied Bacteriology·A W ShelleyI C MacRae
Feb 1, 1986·The Journal of Dairy Research·D J Fairbairn, B A Law

Related Concepts

ELN gene
MME gene
Extracellular
Enzymes, antithrombotic
Clinical Enzyme Tests (Procedure)
Peptide Hydrolases
Chromatography
Endopeptidases
Proteolytic Enzyme
Substrate Specificity

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