✦ LIBER ✦

Purification and properties of soman-hydrolyzing enzyme from human liver

✍ Scribed by Qinding Wang; Manji Sun; Han Zhang; Cuifen Huang 1

Publisher: John Wiley and Sons
Year: 1998
Tongue: English
Weight: 92 KB
Volume: 12
Category: Article
ISSN: 1095-6670
DOI: 10.1002/(sici)1099-0461(1998)12:4<213::aid-jbt3>3.0.co;2-o

No coin nor oath required. For personal study only.

✦ Synopsis

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 lmol/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.

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