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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1984-12-10
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pubmed:abstractText |
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 alpha-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 alpha-subunit of Ni in rat fat cells appear to be homologous, but non-identical peptides.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholera Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside Diphosphate Sugars,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Thionucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
176
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
301-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6386524-Adenosine Diphosphate Ribose,
pubmed-meshheading:6386524-Adenylate Cyclase Toxin,
pubmed-meshheading:6386524-Adipose Tissue,
pubmed-meshheading:6386524-Animals,
pubmed-meshheading:6386524-Bacterial Toxins,
pubmed-meshheading:6386524-Cholera Toxin,
pubmed-meshheading:6386524-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6386524-Female,
pubmed-meshheading:6386524-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:6386524-Guanosine Triphosphate,
pubmed-meshheading:6386524-Liver,
pubmed-meshheading:6386524-Lymphoma,
pubmed-meshheading:6386524-Membrane Proteins,
pubmed-meshheading:6386524-Molecular Weight,
pubmed-meshheading:6386524-NAD,
pubmed-meshheading:6386524-Nucleoside Diphosphate Sugars,
pubmed-meshheading:6386524-Peptide Hydrolases,
pubmed-meshheading:6386524-Pertussis Toxin,
pubmed-meshheading:6386524-Rats,
pubmed-meshheading:6386524-Rats, Inbred Strains,
pubmed-meshheading:6386524-Thionucleotides,
pubmed-meshheading:6386524-Virulence Factors, Bordetella
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pubmed:year |
1984
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pubmed:articleTitle |
Pertussis toxin catalyzes the ADP-ribosylation of two distinct peptides, 40 and 41 kDa, in rat fat cell membranes.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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