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Studies on the antioxidant effect and interaction of diphenyl diselenide and dicholesteroyl diselenide with hepatic delta-aminolevulinic acid dehydratase and isoforms of lactate dehydrogenase.
Kade, I J; Paixão, M W; Rodrigues, O E D; Ibukun, E O; Braga, A L; Zeni, G; Nogueira, C W; Rocha, J B T.
Affiliation
  • Kade IJ; Postgraduate Programme in Biochemical Toxicology, Department of Chemistry, CCNE, Federal University of Santa Maria, CEP 97105-900 Camobi, Santa Maria, RS, Brazil. ijkade@yahoo.com
Toxicol In Vitro ; 23(1): 14-20, 2009 Feb.
Article in En | MEDLINE | ID: mdl-18804525
ABSTRACT
Studies on the interaction of dicholesteroyl diselenide (DCDS) and diphenyl diselenide (DPDS) with hepatic delta-aminolevulinic acid dehydratase (ALA-D) and different isoforms of lactate dehydrogenase (LDH) from different tissues were investigated. In addition, their antioxidant effects were tested in vitro by measuring the ability of the compounds to inhibit the formation of hepatic thiobarbituric acid reactive species (TBARS) induced by both iron (II) and sodium nitroprusside (SNP). The results show that while DPDS markedly inhibited the formation of TBARS induced by both iron (II) and SNP, DCDS did not. Also, the activities of hepatic delta-aminolevulinic acid dehydratase (ALA-D) and different isoforms of lactate dehydrogenase (LDH) were significantly inhibited by both DPDS and DCDS. Moreover, we further observed that the in vitro inhibition of different isoforms of lactate dehydrogenase by DCDS and DPDS likely involves the modification of the groups at the NAD+ binding site of the enzyme. Since organoselenides interacts with thiol groups on proteins, we conclude that the inhibition of different isoforms of lactate dehydrogenase by DPDS and DCDS possibly involves the modification of the thiol groups at the NAD+ binding site of the enzyme.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Benzene Derivatives / Cholesterol / Organoselenium Compounds / Enzyme Inhibitors / Porphobilinogen Synthase / L-Lactate Dehydrogenase / Liver / Antioxidants Limits: Animals Language: En Journal: Toxicol In Vitro Journal subject: TOXICOLOGIA Year: 2009 Document type: Article Affiliation country: Brazil

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Benzene Derivatives / Cholesterol / Organoselenium Compounds / Enzyme Inhibitors / Porphobilinogen Synthase / L-Lactate Dehydrogenase / Liver / Antioxidants Limits: Animals Language: En Journal: Toxicol In Vitro Journal subject: TOXICOLOGIA Year: 2009 Document type: Article Affiliation country: Brazil