- Results for your query on August 15, 1999:
- Search all fields for: methyl sulfonyl methane
- Published in 1966 through 1999
Documents: 1 to 3 of 3
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NLM database Documents
Record 1 from database: MEDLINE
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- Title
- Species variations in the sensitivity of the endoplasmic reticulum to the
herbicide 1.1.1. trifluoro-N-(2-methyl-4-phenyl sulfonyl phenyl) methane
sulfonamide.
- Author
- Thabrew MI; Emerole GO
- Address
-
- Source
- Comp Biochem Physiol C, 1983, 74:2, 473-6
- Abstract
- 1. The effects of the herbicide 1.1.1. trifluoro-N-(2-methyl-4-phenyl
sulfonyl phenyl) methane sulfonamide on the drug metabolising enzyme
activities in livers of rat, mouse and guinea pig have been compared. 2. In
all three animal models, the herbicide increased the activities of both
aniline hydroxylase and p-aminopyrine demethylase. The greatest inductive
effect was seen in the rat, while the least effect was evident in the guinea
pig. 3. In mouse and guinea pig, 1.1.1. trifluoro-N-(2-methyl-4-phenyl
sulfonyl phenyl) methane sulfonamide had no effect on the soluble or
microsomal epoxide hydratases or the glutathione S-transferases. In the rat,
however, the herbicide significantly decreased the microsomal epoxide
hydratase activity, as well as the soluble and microsomal glutathione S-transferase
activities. 4. These results are discussed in relation to factors
responsible for species differences in the response to foreign compounds.
- Language of Publication
- English
- Unique Identifier
- 83208284
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- MeSH Heading (Major)
- Endoplasmic Reticulum|*DE/EN; Herbicides|*PD; Liver|*DE/UL; Sulfones|*PD
- MeSH Heading
- Animal; Guinea Pigs; Male; Mice; Microsomes, Liver|EN; Rats; Rats, Inbred
Strains; Species Specificity
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0742-8413
- Country of Publication
- ENGLAND
Record 2 from database: MEDLINE
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- Title
- Effect of 1.1.1 trifluoro-N-(2-methyl-4-phenyl sulfonyl) methane
sulfonamide (Destun 50WP) on rat hepatic microsomal enzymes, aniline
hydroxylase and amino-pyrine N-demethylase.
- Author
- Thabrew MI; Emerole GO
- Address
-
- Source
- Eur J Drug Metab Pharmacokinet, 1983 Oct, 8:4, 321-7
- Abstract
- Investigations have been carried out to determine the effects of the
herbicide 1.1.1 trifluoro-N-(2-methyl-4-phenyl sulfonyl) methane sulfonamide
(Destun) on some hepatic microsomal drug metabolizing enzymes in rat.
Administration of 100 mg herbicide/kg rat (i.p. or oral) resulted in a
stimulation of aniline hydroxylase and p-aminopyrene N-demethylase
activities by 1.3 fold and 1.6 fold respectively. A dose-related increase in
enzyme activities was observed with a maximum effect at about 100 mg Destun/kg
rat. The increased microsomal protein content, liver weight: body weight
ratio and decreased sleeping time in the herbicide-treated animals indicated
the possibility of Destun being an "inducer". Results of
investigations on the kinetic properties of aniline hydroxylase and p-aminopyrene-N-demethylase
on administration of Destun suggests that in addition to its inducer effect,
the herbicide could stimulate the enzyme activities by decreasing the
affinity of these enzymes for their respective substrates.
- Language of Publication
- English
- Unique Identifier
- 84182654
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- MeSH Heading (Major)
- Aminopyrine N-Demethylase|*ME; Aniline Hydroxylase|*ME; Aryl Hydrocarbon
Hydroxylases|*ME; Herbicides|*PD; Microsomes, Liver|DE/*EN; Sulfones|*PD
- MeSH Heading
- Animal; Enzyme Induction|DE; Male; Phenobarbital|ME/PD; Rats; Rats, Inbred
Strains; Sleep|DE
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0398-7639
- Country of Publication
- FRANCE
Record 3 from database: MEDLINE
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- Title
- [Electrophoretic study of aged butyrylcholinesterase after inhibition by
soman]
- Author
- Masson P; Marnot B; Lombard JY; Morelis P
- Address
-
- Source
- Biochimie, 1984 Mar, 66:3, 235-49
- Abstract
- The following states of purified tetrameric form (C4) of human plasma
butyrylcholinesterase were studied by electrophoretic techniques: native,
inhibited by soman and by methane sulfonyl fluoride and soman-aged. In order
to detect a significant conformational change of the aged cholinesterase as
compared to the non-inhibited (native) species, enzymes were treated with a
set of bifunctional reagents (diimidates) of different chain lengths. After
denaturation, the cross-link products were subjected to sodium dodecyl-sulfate
polyacrylamide gel electrophoresis. The peak areas of the cross-linked
species and the parameters of cross-linkability were calculated from
densitometric data, versus the maximal effective reagent length. The effect
of occupancy of the esteratic site by substituted phosphonyl group and by
methyl-sulfonyl residue on the binding activity of the anionic site was
studied by affinity electrophoresis at varying temperatures with
immobilized-procaïnamide as ligand. Apparent dissociation-constants of the
enzyme-ligand complexes were estimated from measurement of mobilities versus
ligand concentration. Corresponding thermodynamic quantities were calculated
from Van't Hoff plots and basic thermodynamic equations. The reactivity of
aged-cholinesterase with diimidates was similar to that of the native
enzyme. Affinity for immobilized-procaïnamide was slightly lowered in aged
and inhibited enzymes as compared to the native and sulfonylated enzymes. As
for the ligand-induced isomerization of anionic site (A----B), revealed by
affinity electrophoresis, the ligand concentration at the midpoint of
transition (A = 0,5) was slightly greater for the aged enzyme than for the
native one. From these results, the following conclusions can be drawn: the
dealkylation of soman-cholinesterase conjugate (aging) does not seem to
induce structural changes detectable in the cross-linkability of lysyle
residues at the subunit interfaces and on the surface of the tetrameric
enzyme. On the other hand, the affinity of the anionic site and ligand-induced
isomerization process are altered in soman-inhibited and aged enzymes. These
data suggest the occurrence of a weak conformational change of the active
center and/or the formation of non-covalent bonds between the
methylphosphonyl residue and side chain groups as a result of the
dealkylation reaction.
- Language of Publication
- French
- Unique Identifier
- 84257758
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- MeSH Heading (Major)
- Butyrylcholinesterase|*; Cholinesterase Inhibitors|*PD; Cholinesterases|*;
Organophosphorus Compounds|*PD; Soman|*PD
- MeSH Heading
- Cross-Linking Reagents|PD; Electrophoresis, Polyacrylamide Gel; English
Abstract; Human; Mathematics; Mesylates|PD; Protein Conformation
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0300-9084
- Country of Publication
- FRANCE
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