| Literature DB >> 11898341 |
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.Entities:
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Year: 2001 PMID: 11898341 DOI: 10.1007/bf02817995
Source DB: PubMed Journal: Folia Microbiol (Praha) ISSN: 0015-5632 Impact factor: 2.099