Characterization of two mu class glutathione S-transferases from guinea pig lens.
Glutathione S-transferase (GST) plays an important role in the detoxifications of foreign electrophiles. Two GSTs of class mu from guinea pig lens were purified with Sephacryl S-100 gelfiltration, S-Hexyl glutathione Agarose affinity and Q-Sepharose anion exchange chromatographies. These GSTs (GST-A and B) showed similar relative molecular masses of 22.9 and 22.5 kDa, respectively. Two protein bands which crossreacted with anti GSTYb1 (GST 3-3) were detected in lens cytosolic crude extract on Western blotting and they showed Mrs corresponding to the purified enzymes. These GSTs showed a strong resistance against H2O2, 1,2-naphthoquinone and superoxide anion consistent with the other GSTs in class mu from animal tissues.
Noda
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Faculty of Pharmaceutical Sciences, Osaka University, Suita, Japan.
Adachi
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H
Nanjo
H
H
Terada
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T
D000818:Animals; D015153:Blotting, Western; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006168:Guinea Pigs; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007908:Lens, Crystalline / Q000201:enzymology*; D009285:Naphthoquinones / Q000494:pharmacology; D013379:Substrate Specificity; D013481:Superoxides / Q000494:pharmacology
D004791:Enzyme Inhibitors; D009285:Naphthoquinones; D013481:Superoxides; C040756:1,2-naphthoquinone; D006861:Hydrogen Peroxide; D005982:Glutathione Transferase