Premium
Purification and properties of soman‐hydrolyzing enzyme from human liver
Author(s) -
Wang Qinding,
Sun Manji,
Zhang Han,
Huang Cuifen
Publication year - 1998
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/(sici)1099-0461(1998)12:4<213::aid-jbt3>3.0.co;2-o
Subject(s) - soman , enzyme , chemistry , biochemistry , liver enzyme , chromatography , biology , acetylcholinesterase , endocrinology
A soman‐hydrolyzing enzyme (soman‐ase) was purified from human liver. The humansomanase is capable of hydrolyzing pinacolyl meth‐ylphosphonofluoridate (soman), diisopropylphos‐phorofluoridate (DFP), and ethyl‐N‐dimethyl phos‐phoramidocyanidate (Tabun) with P–F or P–CNbonding, but not ethyl (S‐2‐diisopropylaminoethyl)methylphosphonothiolate (VX) and diethyl‐ p ‐nitro‐phosphenylphosphate (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. © 1998 John Wiley & Sons, Inc. J Biochem Toxicol 12: 213–217, 1998