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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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Bibliographic Details
Published in:Biochemical systematics and ecology 2004-02, Vol.32 (2), p.169-178
Main Authors: Nóvoa-Valiñas, M.Carmen, Pérez-López, Marcos, Melgar-Riol, M.Julia
Format: Article
Language:English
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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.
ISSN:0305-1978
1873-2925
DOI:10.1016/S0305-1978(03)00138-8