Endogenous inhibitor of the ADP‐ribosylation of (a) G‐protein(s) as catalyzed by pertussis toxin is present in rat liver
- 4 July 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 234 (1) , 27-30
- https://doi.org/10.1016/0014-5793(88)81295-x
Abstract
The inhibitor activity of the ADP‐ribosylation of (a) G‐protein(s) as catalyzed by pertussis toxin was found in the membrane extract of rat liver. The inhibitor activity was found in the fractions of DEAE‐Sephacel column chromatography at 50–120 mM NaCl. The inhibitor activity is not due to the degradation of NAD nor to the reverse reaction of pertussis toxin (removal of incorporated ADP‐ribose). The present result suggests the presence of an endogenous inhibitor of the ADP‐ribosylation reaction of (a) G‐protein(s).Keywords
This publication has 12 references indexed in Scilit:
- Identification of a new GTP-binding protein. A Mr = 43,000 substrate for pertussis toxin.Journal of Biological Chemistry, 1987
- A new GTP‐binding protein in brain tissues serving as the specific substrate of islet‐activating protein, pertussis toxinFEBS Letters, 1987
- An NAD: Cysteine ADP-Ribosyltransferase Is Present in Human ErythrocytesThe Journal of Biochemistry, 1987
- The stimulatory guanine-nucleotide regulatory unit of adenylate cyclase from bovine cerebral cortex ADP-ribosylation and purificationBiochemical Journal, 1987
- Conversion of adrenergic mechanism from an alpha- to a beta-type during primary culture of rat hepatocytes. Accompanying decreases in the function of the inhibitory guanine nucleotide regulatory component of adenylate cyclase identified as the substrate of islet-activating protein.Journal of Biological Chemistry, 1984
- Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain.Journal of Biological Chemistry, 1984
- Purification and properties of the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase.Journal of Biological Chemistry, 1984
- ADP-ribosylation of transducin by islet-activation protein. Identification of asparagine as the site of ADP-ribosylation.Journal of Biological Chemistry, 1984
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970