author_facet Clark, A. G.
Smith, J. N.
Speir, T. W.
Clark, A. G.
Smith, J. N.
Speir, T. W.
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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publisher Portland Press Ltd.
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series Biochemical Journal
source_id 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>
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id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Mi9iajEzNTAzODU
imprint Portland Press Ltd., 1973
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)
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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