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Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotony...
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Zeitschriftentitel: | Biochemical Journal |
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Personen und Körperschaften: | , , |
In: | Biochemical Journal, 135, 1973, 3, S. 385-392 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Portland Press Ltd.
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Schlagwörter: |
author_facet |
Clark, A. G. Smith, J. N. Speir, T. W. Clark, A. G. Smith, J. N. Speir, T. W. |
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author |
Clark, A. G. Smith, J. N. Speir, T. W. |
spellingShingle |
Clark, A. G. Smith, J. N. Speir, T. W. Biochemical Journal Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates Cell Biology Molecular Biology Biochemistry |
author_sort |
clark, a. g. |
spelling |
Clark, A. G. Smith, J. N. Speir, T. W. 0264-6021 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj1350385 <jats:p>1. Enzymes catalysing the reaction between GSH and methylparathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine were separated by (NH4)2SO4 precipitation from homogenates of sheep, rat and mouse livers and from homogenates of cockroaches, houseflies and grass grubs. 2. Electrofocusing of the preparations from each of these species separated a number of zones, each of which catalysed the reaction of GSH with all three substrates. 3. Ion-exchange chromatography on CM-cellulose also separated a number of fractions in which activity towards the three substrates coincided. 4. In both separation methods patterns of the activities were consistent with the presence in all species of several GSH transferases each having a degree of cross specificity towards the three substrates.</jats:p> Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl <i>p</i>-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and <i>S</i>-crotonyl-<i>N</i>-acetylcysteamine as substrates Biochemical Journal |
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10.1042/bj1350385 |
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Online Free |
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Chemie und Pharmazie Biologie |
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ElectronicArticle |
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Portland Press Ltd., 1973 |
imprint_str_mv |
Portland Press Ltd., 1973 |
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0264-6021 |
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0264-6021 |
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English |
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1973 |
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Portland Press Ltd. |
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Biochemical Journal |
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49 |
title |
Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
title_unstemmed |
Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
title_full |
Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
title_fullStr |
Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
title_full_unstemmed |
Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
title_short |
Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
title_sort |
cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl <i>p</i>-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and <i>s</i>-crotonyl-<i>n</i>-acetylcysteamine as substrates |
topic |
Cell Biology Molecular Biology Biochemistry |
url |
http://dx.doi.org/10.1042/bj1350385 |
publishDate |
1973 |
physical |
385-392 |
description |
<jats:p>1. Enzymes catalysing the reaction between GSH and methylparathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine were separated by (NH4)2SO4 precipitation from homogenates of sheep, rat and mouse livers and from homogenates of cockroaches, houseflies and grass grubs. 2. Electrofocusing of the preparations from each of these species separated a number of zones, each of which catalysed the reaction of GSH with all three substrates. 3. Ion-exchange chromatography on CM-cellulose also separated a number of fractions in which activity towards the three substrates coincided. 4. In both separation methods patterns of the activities were consistent with the presence in all species of several GSH transferases each having a degree of cross specificity towards the three substrates.</jats:p> |
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author | Clark, A. G., Smith, J. N., Speir, T. W. |
author_facet | Clark, A. G., Smith, J. N., Speir, T. W., Clark, A. G., Smith, J. N., Speir, T. W. |
author_sort | clark, a. g. |
container_issue | 3 |
container_start_page | 385 |
container_title | Biochemical Journal |
container_volume | 135 |
description | <jats:p>1. Enzymes catalysing the reaction between GSH and methylparathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine were separated by (NH4)2SO4 precipitation from homogenates of sheep, rat and mouse livers and from homogenates of cockroaches, houseflies and grass grubs. 2. Electrofocusing of the preparations from each of these species separated a number of zones, each of which catalysed the reaction of GSH with all three substrates. 3. Ion-exchange chromatography on CM-cellulose also separated a number of fractions in which activity towards the three substrates coincided. 4. In both separation methods patterns of the activities were consistent with the presence in all species of several GSH transferases each having a degree of cross specificity towards the three substrates.</jats:p> |
doi_str_mv | 10.1042/bj1350385 |
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id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Mi9iajEzNTAzODU |
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imprint_str_mv | Portland Press Ltd., 1973 |
institution | DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1 |
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mega_collection | Portland Press Ltd. (CrossRef) |
physical | 385-392 |
publishDate | 1973 |
publishDateSort | 1973 |
publisher | Portland Press Ltd. |
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series | Biochemical Journal |
source_id | 49 |
spelling | Clark, A. G. Smith, J. N. Speir, T. W. 0264-6021 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj1350385 <jats:p>1. Enzymes catalysing the reaction between GSH and methylparathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine were separated by (NH4)2SO4 precipitation from homogenates of sheep, rat and mouse livers and from homogenates of cockroaches, houseflies and grass grubs. 2. Electrofocusing of the preparations from each of these species separated a number of zones, each of which catalysed the reaction of GSH with all three substrates. 3. Ion-exchange chromatography on CM-cellulose also separated a number of fractions in which activity towards the three substrates coincided. 4. In both separation methods patterns of the activities were consistent with the presence in all species of several GSH transferases each having a degree of cross specificity towards the three substrates.</jats:p> Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl <i>p</i>-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and <i>S</i>-crotonyl-<i>N</i>-acetylcysteamine as substrates Biochemical Journal |
spellingShingle | Clark, A. G., Smith, J. N., Speir, T. W., Biochemical Journal, Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates, Cell Biology, Molecular Biology, Biochemistry |
title | Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
title_full | Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
title_fullStr | Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
title_full_unstemmed | Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
title_short | Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
title_sort | cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl <i>p</i>-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and <i>s</i>-crotonyl-<i>n</i>-acetylcysteamine as substrates |
title_unstemmed | Cross-specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitrobenzene and S-crotonyl-N-acetylcysteamine as substrates |
topic | Cell Biology, Molecular Biology, Biochemistry |
url | http://dx.doi.org/10.1042/bj1350385 |