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rdf:type |
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lifeskim:mentions |
umls-concept:C0017963,
umls-concept:C0020960,
umls-concept:C0021469,
umls-concept:C0085979,
umls-concept:C0086376,
umls-concept:C0205332,
umls-concept:C0227525,
umls-concept:C0752348,
umls-concept:C1264633,
umls-concept:C1321758,
umls-concept:C1383501,
umls-concept:C1979928,
umls-concept:C2700400
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pubmed:issue |
16
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pubmed:dateCreated |
1990-9-20
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pubmed:abstractText |
Guinea pig hepatocytes fractionated by differential centrifugation into plasma membrane-enriched, microsomal, and cytosolic fractions were examined for their content of alpha and beta subunits of heterotrimeric GTP-binding proteins (G proteins) involved in signal transduction. alpha subunits of stimulatory (Gs) and inhibitory (Gi) proteins were detected by immunoblots with antisera reactive with the carboxyl-terminal decapeptide regions of these proteins. Unexpectedly, antisera (including immunopurified) to the alpha subunit but not the beta subunit reacted with a band of 100-kDa proteins in both the microsomal and cytosolic fractions. The immunoreactive 100-kDa proteins are not substrates for ADP-ribosylation catalyzed by pertussis toxin, cholera toxin, or diptheria toxin. Protease digests of the 100-kDa proteins yielded immunoreactive peptides that are distinctly different from those obtained from protease digests of alpha subunits of heterotrimeric G proteins. The 100-kDa protein(s) reactive with antisera to Gi alpha subunit bind to GTP-agarose but not to ATP-agarose. It is concluded that the immunoreactive 100-kDa proteins in microsomal and cytosolic fractions are structurally distinct G proteins from those linked to receptors in the plasma membrane and other G proteins such as elongation factor 2. Conceivably, the 100-kDa proteins represent a new class of G proteins.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-1091638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-2105498,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-215787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-228287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-2407590,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-2494307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-2510151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-2515926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-2536591,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-2539152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-2670240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-2836559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-2852763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-3014523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-3092218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-3113327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-3132454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-3134354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-3155263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-320200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-3896232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-446743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-4630105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-4867665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-4900611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-6136509,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-6142883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-6145704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-6203340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-6654915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-6855576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696725-942051
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6321-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1696725-Adenosine Diphosphate Ribose,
pubmed-meshheading:1696725-Animals,
pubmed-meshheading:1696725-Cholera Toxin,
pubmed-meshheading:1696725-Chromatography, Affinity,
pubmed-meshheading:1696725-Cytosol,
pubmed-meshheading:1696725-Diphtheria Toxin,
pubmed-meshheading:1696725-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1696725-Epitopes,
pubmed-meshheading:1696725-GTP-Binding Proteins,
pubmed-meshheading:1696725-Guinea Pigs,
pubmed-meshheading:1696725-Immune Sera,
pubmed-meshheading:1696725-Liver,
pubmed-meshheading:1696725-Macromolecular Substances,
pubmed-meshheading:1696725-Male,
pubmed-meshheading:1696725-Microsomes, Liver,
pubmed-meshheading:1696725-Molecular Weight,
pubmed-meshheading:1696725-Pertussis Toxin,
pubmed-meshheading:1696725-Virulence Factors, Bordetella
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pubmed:year |
1990
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pubmed:articleTitle |
Microsomal and cytosolic fractions of guinea pig hepatocytes contain 100-kilodalton GTP-binding proteins reactive with antisera against alpha subunits of stimulatory and inhibitory heterotrimeric GTP-binding proteins.
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pubmed:affiliation |
Laboratory of Cellular and Molecular Pharmacology, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709.
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pubmed:publicationType |
Journal Article
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