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Pertussis toxin catalyzes the ADP‐ribosylation of two distinct peptides, 40 and 41 kDa, in rat fat cell membranes
Author(s) -
Malbon Craig C.,
Rapiejko Peter J.,
Garciá-Sáinz J.Adolfo
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81184-9
Subject(s) - adp ribosylation , pertussis toxin , toxin , membrane , chemistry , biochemistry , cell , cell membrane , microbiology and biotechnology , biology , enzyme , receptor , g protein , nad+ kinase
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 (N i ). Incubating membranes of rat fat cells with pertussis toxin and [ 32 P]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 [ 32 P]NAD + and pertussis toxin. The 40‐kDa substrate for pertussis toxin‐catalyzed ADP‐ribosylation and the α‐subunit of N i in rat fat cells appear to be homologous, but non‐identical peptides.