PMID: 11898341Mar 20, 2002Paper

Production, purification and characterization of intracellular alanylaminopeptidase of Pseudomonas sp

Folia Microbiologica
U Jankiewicz, W Bielawski

Abstract

The soil bacterium Pseudomonas sp. was found to synthesize an aminopeptidase that prefers Ala-beta-naphtylamide as substrate. The enzyme was purified 660-fold by ammonium sulfate fractionation, preparative electrophoresis, ion exchange chromatography on Protein-Pak Q 8 HR and molecular sieving chromatography on Zorbax SE-250. When purified to homogeneity, the enzyme was shown to be a monomeric protein with a molar mass of 65 kDa; it showed a maximum activity at pH 7.5 and 45 degrees C.

References

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Citations

Related Concepts

Molecular Sieve Chromatography
Ion-Exchange Chromatography Procedure
Electrophoresis
Fractional Precipitation
Hydrogen-Ion Concentration
Pseudomonas
Substrate Specificity
2-Naphthylamine
Aminooligopeptidase

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