δ-Aminolevulinate Dehydratase Inhibition by 2, 3-Dimercaptopropanol is Mediated by Chelation of Zinc from a Site Involved in Maintaining Cysteinyl Residues in a Reduced State-Reference-Cited by-同舟云学术

δ-Aminolevulinate Dehydratase Inhibition by 2, 3-Dimercaptopropanol is Mediated by Chelation of Zinc from a Site Involved in Maintaining Cysteinyl Residues in a Reduced State

Published:1998-09 Issue:3 Volume:83 Page:95-103
ISSN:0901-9928
Container-title:Pharmacology & Toxicology
language:en
Short-container-title:

Author:

Emanuelli Tatiana,Rocha João Batista T.,Pereira Maria Ester,Nascimento Paulo C.,Souza Diogo O. G.,Beber Flávio A.

Publisher

Wiley

Subject

Health, Toxicology and Mutagenesis,Pharmacology,Toxicology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1600-0773.1998.tb01451.x/fullpdf

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3. δ-Aminolevulinate dehydratase inhibition by ascorbic acid is mediated by an oxidation system existing in the hepatic supernatant. Internat;Beber;J. Vit. Nutr. Res.,1998

4. Lead binding to δ-aminolevulinic acid dehydratase (ALAD) in human erythrocytes;Bergdahl;Pharmacology & Toxicology,1997

5. Mechanism of porphobilinogen synthase. Requirement of Zn2+ for enzyme activity;Bevan;J. Biol. Chem.,1980

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