Characterization of a soluble mouse liver enzyme capable of hydrolyzing diisopropyl phosphorofluoridate.
Chem Biol Interact
; 119-120: 251-6, 1999 May 14.
Article
in En
| MEDLINE
| ID: mdl-10421459
ABSTRACT
A novel mouse liver soluble fraction DFPase which has organophosphatase activities with sarin, soman and tabun, was purified and characterized. However, it lacks paraoxonase and arylesterase activities with paraoxon and phenyl acetate, respectively. This DFPase closely resembles and may be identical with the one purified by Little et al. in 1989 from the soluble fraction of rat liver, based on its substrate specificity, size (approximately 39 kDa) and its stimulation by several metal ions, namely magnesium, manganese and cobalt. Sequencing of our purified mouse liver DFPase showed it to be identical in its amino acid sequence with the recently identified senescence marker protein-30 (SMP-30) by Fujita et al. in 1996. Other senescence marker proteins possessing high structural homology with the mouse SMP-30 have also been found and sequenced from human and rat livers. There is no structural homology between the senescence marker protein family and the group of mammalian paraoxonases. Thus, it is clear that there are at least two distinct, unrelated families of mammalian liver enzymes that share DFPase activity.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Phosphoric Triester Hydrolases
/
Esterases
/
Isoflurophate
/
Liver
Limits:
Animals
/
Humans
Language:
En
Journal:
Chem Biol Interact
Year:
1999
Document type:
Article
Affiliation country:
United States