Interaction of divalent metal lons with normal and lead-inhibited human erythrocytic porphobilinogen synthase in vitro-Reference-Cited by-同舟云学术

Interaction of divalent metal lons with normal and lead-inhibited human erythrocytic porphobilinogen synthase in vitro

Published:1987-06 Issue:1 Volume:89 Page:9-18
ISSN:0041-008X
Container-title:Toxicology and Applied Pharmacology
language:en
Short-container-title:Toxicology and Applied Pharmacology

Author:

Farant Jean-Pierre,Wigfield D.C.

Publisher

Elsevier BV

Subject

Pharmacology,Toxicology

Reference25 articles.

1. Antagonistic effect of zinc in relatively high concentrations on inhibition of ALA-dehydratase activity by heavy metals in vitro;Abdulla;IRCS Med. Sci.: Libr. Compend,1973

2. Mechanism of porphobilinogen synthase;Barnard;J. Biol. Chem.,1977

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

4. Un semplice metodo per la determinazione della δ-aminolevulinicodeitrase nel sangue: Campartamento dell enzima nell' intossicazione saturina;Bonsignore;Med. Lav.,1965

5. Zinc, an essential metal ion for beef liver aminolevulinate dehydratase;Cheh,1973

Cited by 8 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Effect of cadmium binding form on rabbit aminolevulinate dehydratase in high molecular weight fraction of rainbow trout liver;Fisheries Science;2010-04-08

2. Anemia Induced by Cadmium Intoxication;Nippon Eiseigaku Zasshi (Japanese Journal of Hygiene);2007

3. Hematopoietic System;Metal Toxicology;1995

4. Porphyrin Metabolism as Indicator of Metal Exposure and Toxicity;Toxicology of Metals;1995

5. Method for preserving erythrocytic δ-aminolevulinic acid dehydratase activity that facilitates population studies on lead intoxication;Journal of Applied Toxicology;1994-09