Purification and Properties of Mouse Serum Carboxylic Ester Hydrolase (EC 3.1.1.1)

摘要

The purification procedure and properties of mouse serum carboxylic ester hydrolase are reported. The enzyme purified using hydrophobic interaction chromatography followed by anion exchange fractionation and chromatofocusing. The purity of the enzyme was assessed by polyacrylamide gel electrophoresis and isoelectric focusing. The effect of various ions organophosphate and carbamate anticholinesterases and CBDP on the carboxylic ester hydrolase activity were examined. Generally the organophosphate anticholinesterases, with the exception of VX, were potent inhibitors of carboxylic ester hydrolase activity whereas the carbamate, physostigmine, was a poor inhibitor. The various ions inhibited carboxylic ester hydrolase activity. None of the ions stimulated carboxylic ester hydrolase activity. Further research is in progress investigating the interaction of nerve agents with carboxylic ester hydrolase and developing purification schemes for carboxylic ester hydrolase from other sources. Keywords: Enzymes, Biochemistry; Assays; Stains(biology).