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Hepatic glutathione S-transferases from lamprey ( Petromyzom marinus): purification and characterization
Glutathione S-transferases constitute a very important family of biotransformation enzymes, which catalyse the conjugation of glutathione to a broad spectrum of xenobiotics. In this study, cytosolic glutathione S-transferases enzymes were purified from lamprey ( Petromyzon marinus) liver, using an a...
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Published in: | Biochemical systematics and ecology 2004-02, Vol.32 (2), p.169-178 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Glutathione
S-transferases constitute a very important family of biotransformation enzymes, which catalyse the conjugation of glutathione to a broad spectrum of xenobiotics. In this study, cytosolic glutathione
S-transferases enzymes were purified from lamprey (
Petromyzon marinus) liver, using an affinity chromatography method. Enzymatic activity was determined towards 1-chloro-2,4-dinitrobenzene, ethacrynic acid and 1,2-dichloro-4-nitrobenzene. The application of a HPLC system associated to electrospray ionization mass spectrometry allowed the identification of three different subunits, with
Mrs between 22,300 and 25,300 Da. The one with the low Mrs was the main form, with a retention time of 29.5 min, a pi-related class isoenzyme. |
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ISSN: | 0305-1978 1873-2925 |
DOI: | 10.1016/S0305-1978(03)00138-8 |