Effect of self-association on activity of an ADP-ribosyltransferase from turkey erythrocytes. Conversion of inactive oligomers to active protomers by chaotropic salts.-Reference-Cited by-同舟云学术

Effect of self-association on activity of an ADP-ribosyltransferase from turkey erythrocytes. Conversion of inactive oligomers to active protomers by chaotropic salts.

Published:1981-11 Issue:22 Volume:256 Page:11452-11456
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Moss J.,Stanley S.J.,Osborne J.C.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference26 articles.

1. Poly (ADP-Ribose) and ADP-Ribosylation of Proteins

2. Mechanism of cholera toxin action: Covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system

3. ADP-ribosylation of membrane proteins catalyzed by cholera toxin: basis of the activation of adenylate cyclase.

4. Genetic evidence that cholera toxin substrates are regulatory components of adenylate cyclase.

5. Adenosine Diphosphate-Ribosylation of Adenylate Cyclase Catalyzed by Heat-Labile Enterotoxin of Escherichia coli: Comparison with Cholera Toxin

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