Results for your query on August 15, 1999:
Search all fields for: methyl sulfonyl methane
Published in 1966 through 1999
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1 Thabrew MI, et al; 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. (Comp Biochem Physiol C, 1983, Abstract available) [MEDLINE]
2 Thabrew MI, et al; 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. (Eur J Drug Metab Pharmacokinet, 1983 Oct, Abstract available) [MEDLINE]
3 Masson P, et al; [Electrophoretic study of aged butyrylcholinesterase after inhibition by soman] (Biochimie, 1984 Mar, Abstract available) [MEDLINE]

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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