Pertussis toxin catalyzes the ADP‐ribosylation of two distinct peptides, 40 and 41 kDa, in rat fat cell membranes
- 29 October 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 176 (2), 301-306
- https://doi.org/10.1016/0014-5793(84)81184-9
Abstract
Pertussis toxin catalyzes the ADP-ribosylation of a single 41-kDa peptide of membranes prepared from rat hepatocytes, S49 mouse lymphoma wild-type and cyc-mutant cells. This 41-kDa peptide has been shown to be the α-subunit of the inhibitory, guanine nucleotide binding regulatory component of adenylate cyclase (Ni). Incubating membranes of rat fat cells with pertussis toxin and [32P]NAD+ radiolabels a 41- and a 40-kDa peptide. Possible homologies between these peptides were investigated by comparing the electrophoretic patterns of proteolytic fragments derived from each of them that are radiolabeled by [32P]NAD+ and pertussis toxin. The 40-kDa substrate for pertussis toxin-catalyzed ADP-ribosylation and the α-subunit of Ni in rat fat cells appear to be homologous, but non-identical peptides.Keywords
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