Purification and Properties of Soman-Hydrolyzing Enzyme from Human Liver

Qingding Wang, Manji Sun, Han Zhang, Cuifen Huang

Research output: Contribution to journalArticlepeer-review

20 Citations (SciVal)


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 languageEnglish
Pages (from-to)213-217
Number of pages5
JournalJournal of Biochemical and Molecular Toxicology
Issue number4
StatePublished - 1998


  • Human Liver
  • Organophosphate Anhydrase
  • Properties
  • Purification
  • Somanase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Toxicology
  • Health, Toxicology and Mutagenesis


Dive into the research topics of 'Purification and Properties of Soman-Hydrolyzing Enzyme from Human Liver'. Together they form a unique fingerprint.

Cite this