title: Production, purification and characterization of intracellular alanylaminopeptidase of Pseudomonas sp.
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.
authors.affiliation: Department of Biochemistry, Warsaw Agricultural University, Warsaw, Poland.
authors.forename: U
authors.initials: U
authors.lastname: Jankiewicz
authors.forename: W
authors.initials: W
authors.lastname: Bielawski
mesh_terms: D015081:2-Naphthylamine / Q000378:metabolism; D018826:CD13 Antigens / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004586:Electrophoresis; D005590:Fractional Precipitation; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D015081:2-Naphthylamine; D018826:CD13 Antigens