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