The Comparative Literature Syndrome

Aldridge, A. Owen

doi:10.1111/j.1540-4781.1969.tb04574.x

Cited by 6 publications

(6 citation statements)

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“…Figure 1). Different ratios of metabolic products in the rat may be a consequence of detoxification via P-O-vinyl bond fission (route b, Figure 1) by an Aor B-type esterase (Aldridge, 1953). B esterases are inhibited by organophosphates (Heath, 1961), the reaction being of the type, In this case, HX would be the enol form of 2,4,5trichlorophenacyl chloride which would be metabolized further to the observed products (Hutson et al, 1967).…”

Section: Resultsmentioning

confidence: 99%

Metabolism of 2-chloro-1-(2,4,5-trichlorophenyl)vinyl dimethyl phosphate in the dog and rat

Akintonwa¹,

Hutson²

1967

J. Agric. Food Chem.

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Section: Resultsmentioning

confidence: 99%

Metabolism of 2-chloro-1-(2,4,5-trichlorophenyl)vinyl dimethyl phosphate in the dog and rat

Akintonwa¹,

Hutson²

1967

J. Agric. Food Chem.

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“…Arylester hydrolase (EC 3.1.1.2), commonly referred to as paraoxonase, has as substrates a range of toxic organophosphates and organophosphinates (Aldridge, 1953;Grothusen et al, 1986). Because of its target substrates, arylester hydrolase is an important enzyme in xenobiotic organophosphorus detoxication and in environmental detoxification.…”

Section: Introductionmentioning

confidence: 99%

Partial purification of rabbit serum arylester hydrolase

Zimmerman¹,

Brown²

1986

J. Agric. Food Chem.

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Arylester hydrolase has been partially purified from rabbit serum to a specific activity matching or exceeding all previous reports. Calcium ion is absolutely required for activity. The widely reported rapid loss of arylester hydrolase activity was overcome by combining this Ca2+ requirement with the presence of 0.02% sodium azide. A method has also been devised to store the enzyme for long periods of time (years). During size exclusion chromatography, the enzyme behaved as if it had a molecular weight of 180-200 kDa. SDS-polyacrylamide gel electrophoresis showed two bands of low molecular weight (40-45 and 47-54 kDa) directly correlated with enzymatic activity, suggesting a possible 2ß2 structure for the native enzyme.

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“…Enzymes involved in detoxification of organophosphate and carbamate insecticides have been extensively investigated with mammalian plasmata and livers. Aldridge (1953) discovered that serum esterases can be divided into two major groups by using an organophosphate inhibitori.e., the A, or aryl esterases, which are not only unaffected by 10" 3M paraoxon but degrade the phosphate, and the B, or aliesterase, which is inhibited by 10"7M paraoxon.…”

mentioning

confidence: 99%

Esterases of mouse brain active in hydrolyzing organophosphate and carbamate insecticides

Sakai¹,

Matsumura²

1968

J. Agric. Food Chem.

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A number of hydrolytic enzymes of mouse brain are detected by a thin-layer agar gel electrophoresis technique. Each of the 13 bands of esterase activity was tested against various substrates, including insecticidal, radiolabeled organophosphates and carbamates, to characterize the abilities of these esterases to degrade these insecticides and their analogs. Three cathodally moving and eight anodally moving bands show appreciable amounts of insecticide-degrading activity. The latter bands can be subdivided into three major groups, one of which is particularly active in hydrolyzing malathion carboxylesters. Organophosphate and carbamate insecticides owe

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The Comparative Literature Syndrome

Cited by 6 publications

References 0 publications

Metabolism of 2-chloro-1-(2,4,5-trichlorophenyl)vinyl dimethyl phosphate in the dog and rat

Metabolism of 2-chloro-1-(2,4,5-trichlorophenyl)vinyl dimethyl phosphate in the dog and rat

Partial purification of rabbit serum arylester hydrolase

Esterases of mouse brain active in hydrolyzing organophosphate and carbamate insecticides

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