PII: S1532-0456(02)00003-0
Abstract In the present report, an efficient method for isolating multiple cytosolic forms of glutathione S-transferases from liver and kidney cytosolic samples of two salmonid species (brown trout and Atlantic salmon) is described, and some of the multiple properties of these enzymes are presented....
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ftciteseerx:oai:CiteSeerX.psu:10.1.1.1055.2009 2023-05-15T15:31:58+02:00 PII: S1532-0456(02)00003-0 M C Novoa-Valinas M Perez-Lopez M J Melgar The Pennsylvania State University CiteSeerX Archives 2002 application/pdf http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.1055.2009 http://www.eweb.unex.es/eweb/toxicologia/Publis%20pdf%20Marcos/Comparative%20GST.pdf en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.1055.2009 http://www.eweb.unex.es/eweb/toxicologia/Publis%20pdf%20Marcos/Comparative%20GST.pdf Metadata may be used without restrictions as long as the oai identifier remains attached to it. http://www.eweb.unex.es/eweb/toxicologia/Publis%20pdf%20Marcos/Comparative%20GST.pdf text 2002 ftciteseerx 2020-04-12T00:21:03Z Abstract In the present report, an efficient method for isolating multiple cytosolic forms of glutathione S-transferases from liver and kidney cytosolic samples of two salmonid species (brown trout and Atlantic salmon) is described, and some of the multiple properties of these enzymes are presented. Glutathione S-transferases were partially purified by low-pressure affinity chromatography on a column with glutathione coupled to agarose, which retained an average of 89.47% of the total activity. The GST activity was appropriated towards CDNB and ETHA as substrates. The application of an HPLC system associated to elestrospray ionization mass spectrometry allowed the identification of five GST cytosolic isoforms, corresponding to subunits with M between 23 700 and 26 900 Da being the main form, with retention time of 17 min, r a p-class-related GST isoenzyme. ᮊ Text Atlantic salmon Unknown |
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ftciteseerx |
language |
English |
description |
Abstract In the present report, an efficient method for isolating multiple cytosolic forms of glutathione S-transferases from liver and kidney cytosolic samples of two salmonid species (brown trout and Atlantic salmon) is described, and some of the multiple properties of these enzymes are presented. Glutathione S-transferases were partially purified by low-pressure affinity chromatography on a column with glutathione coupled to agarose, which retained an average of 89.47% of the total activity. The GST activity was appropriated towards CDNB and ETHA as substrates. The application of an HPLC system associated to elestrospray ionization mass spectrometry allowed the identification of five GST cytosolic isoforms, corresponding to subunits with M between 23 700 and 26 900 Da being the main form, with retention time of 17 min, r a p-class-related GST isoenzyme. ᮊ |
author2 |
The Pennsylvania State University CiteSeerX Archives |
format |
Text |
author |
M C Novoa-Valinas M Perez-Lopez M J Melgar |
spellingShingle |
M C Novoa-Valinas M Perez-Lopez M J Melgar PII: S1532-0456(02)00003-0 |
author_facet |
M C Novoa-Valinas M Perez-Lopez M J Melgar |
author_sort |
M C Novoa-Valinas |
title |
PII: S1532-0456(02)00003-0 |
title_short |
PII: S1532-0456(02)00003-0 |
title_full |
PII: S1532-0456(02)00003-0 |
title_fullStr |
PII: S1532-0456(02)00003-0 |
title_full_unstemmed |
PII: S1532-0456(02)00003-0 |
title_sort |
pii: s1532-0456(02)00003-0 |
publishDate |
2002 |
url |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.1055.2009 http://www.eweb.unex.es/eweb/toxicologia/Publis%20pdf%20Marcos/Comparative%20GST.pdf |
genre |
Atlantic salmon |
genre_facet |
Atlantic salmon |
op_source |
http://www.eweb.unex.es/eweb/toxicologia/Publis%20pdf%20Marcos/Comparative%20GST.pdf |
op_relation |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.1055.2009 http://www.eweb.unex.es/eweb/toxicologia/Publis%20pdf%20Marcos/Comparative%20GST.pdf |
op_rights |
Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
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1766362453464055808 |