Demonstration of choleragen-dependent ADP-ribosylation in whole cells and correlation with the activation of adenylate cyclase
| Autor: | Claus J. Schmitges, Naji Sahyoun, Pedro Cuatrecasas, G. Matthew Hebdon, Harry Le Vine |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Cholera Toxin
Cell Membrane Permeability Erythrocytes Cell Adenylate kinase medicine.disease_cause Cyclase General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound Mice medicine Animals General Pharmacology Toxicology and Pharmaceutics Columbidae Adenosine Diphosphate Ribose Nicotinamide Chemistry Toxin Nucleoside Diphosphate Sugars Erythrocyte Membrane General Medicine Fibroblasts Hydrogen-Ion Concentration NAD Clone Cells Enzyme Activation Membrane medicine.anatomical_structure Biochemistry ADP-ribosylation NAD+ kinase Peptides Adenylyl Cyclases |
| Zdroj: | Life sciences. 26(17) |
| ISSN: | 0024-3205 |
| Popis: | 3T3C 2 mouse fibroblasts rendered permeable to ( α −32 P)NAD + show cholera toxin-dependent labeling of a 45,000 m.w. protein and of a doublet of polypeptides around 52,000 m.w. These same bands are ADP-ribosylated in broken cells. Membranes prepared from pigeon erythrocytes pretreated with choleragen show a decrease in subsequent cholera toxin-specific ADP-ribosylation of a 43,000 m.w. polypeptide. Both whole cell and broken cell adenylate cyclase activation and toxin-specific ADP-ribosylation are reversed specifically by low pH and high concentrations of toxin and nicotinamide in all systems. Thus ADP-ribosylation appears to be relevant to the molecular action of choleragen in whole cells as well as in broken cells. |
| Databáze: | OpenAIRE |
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