[Characterization of Escherichia coli esterase B after separation by chromatography].
Esterase B of Escherichia coli has been purified 56 fold with recovery of 39%. The apparent molecular weight as determined by gel filtration was approximately 57000. The pI as determined by isoelectric focusing was 4.6. This enzyme exhibited Michaelis-Menton kinetics with apparent Km of 0.25 mM for l-naphtyl acetate. It remained stable at 60 degrees C but was sensitive to pH values below 6. The esterase activity was completely inhibited by Di-isopropyl-fluorophosphate (DFP) but was resistant to iodoacetamide and to EDTA.
D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D002850:Chromatography, Gel / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D004492:Edetic Acid / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D007460:Iodoacetamide / Q000494:pharmacology; D007531:Isoflurophate / Q000494:pharmacology; D007700:Kinetics; D008970:Molecular Weight; D009283:Naphthol AS D Esterase / Q000302:isolation & purification / Q000378:metabolism*
D007531:Isoflurophate; D004492:Edetic Acid; D009283:Naphthol AS D Esterase; D002265:Carboxylic Ester Hydrolases; D007460:Iodoacetamide
Caractérisation de l'estérase B d'Escherichia coli après séparation par chromatographie.