Abstract
A soman-hydrolyzing enzyme (somanase) was purified from human liver. The human somanase is capable of hydrolyzing pinacolyl methylphosphonofluoridate (soman), diisopropylphosphorofluoridate (DFP), and ethyl-N-dimethyl phosphoramidocyanidate (Tabun) with P-F or P-CN bonding, but not ethyl (S-2-diisopropylaminoethyl) methylphosphonothiolate (VX) and diethyl-p-nitrophosphenylphosphate (paraoxon) with P-S or P-O bonding. The somanase has been purified 1570-fold with a specific activity of 41.4 μmol/min/mg protein. Its molecular weight is around 58 kDa determined by SDS-PAGE. The somanase could be stimulated by the divalent cations Mn+2, Mg+2, and Co+2, where Co+2 activation is the highest. The requirement of disulfide bonds for the enzyme activity was demonstrated by the inhibition effect of DTT.
Original language | English |
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Pages (from-to) | 213-217 |
Number of pages | 5 |
Journal | Journal of Biochemical and Molecular Toxicology |
Volume | 12 |
Issue number | 4 |
DOIs | |
State | Published - 1998 |
Keywords
- Human Liver
- Organophosphate Anhydrase
- Properties
- Purification
- Somanase
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Toxicology
- Health, Toxicology and Mutagenesis