?-Aminolevulinic Acid Dehydratase Isozymes and Lead Toxicity-Reference-Cited by-同舟云学术

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?-Aminolevulinic Acid Dehydratase Isozymes and Lead Toxicity

Published:1987-12 Issue:1 Mechanisms of Volume:514 Page:23-29
ISSN:0077-8923
Container-title:Annals of the New York Academy of Sciences
language:en
Short-container-title:Ann NY Acad Sci

Author:

ASTRIN K. H.,BISHOP D. F.,WETMUR J. G.,KAUL B.,DAVIDOW B.,DESNICK R. J.

Publisher

Wiley

Subject

History and Philosophy of Science,General Biochemistry, Genetics and Molecular Biology,General Neuroscience

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1749-6632.1987.tb48757.x/fullpdf

Reference44 articles.

1. The Quaternary Structure of -Aminolevulinic Acid Dehydratase from Bovine Liver

2. Dissociation and reassociation of immobilized porphobilinogen synthase: use of immobilized subunits for enzyme isolation.

3. Purification and properties of delta-aminolevulinate dehydrase from human erythrocytes.

4. Mechanism of porphobilinogen synthase. Requirement of Zn2+ for enzyme activity.

5. The role of zinc with special reference to the essential thiol groups in δ-aminolevulinic acid dehydratase of bovine liver

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