PURIFICATION AND PROPERTIES OF MOUSE SERUM CARBOXYLIC ESTER HYDROLASE (EC 3.1.1.1)

Authors
  1. Clement, J.G.
Corporate Authors
Defence Research Establishment Suffield, Ralston ALTA (CAN)
Abstract
The purification procedures and properties of mouse serum carboxylic ester hydrolase (EC 3.1.1.1) are reported. The enzyme was 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 (Na, Ca, Mg, Mn, Cu, K, Zn, Li, Ce, Fe), organophosphate (DFP, soman, sarin, tabun, and VX) and carbamate (physostigmine) anticholinesterases and CBDP(2-/O-cresyl/-4H-l:3:2-benzodioxaphosphorin-2-oxide) 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. TRUNCATED
Report Number
DRES-482 —
Date of publication
15 Jul 1987
Number of Pages
27
DSTKIM No
87-03266
CANDIS No
52064
Format(s):
Hardcopy;Originator's fiche received by DSIS

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