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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1984-1-7
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pubmed:abstractText |
Under reducing conditions (5% beta-mercaptoethanol) the mammalian beta-adrenergic receptor binding site from both beta 1 (porcine heart membranes) and beta 2 receptors (hamster lung and rat erythrocyte membranes) appears to reside on peptides of Mr 62,000-65,000 as determined by photoaffinity labeling with p-azido-m-[125I]iodobenzylcarazolol and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. When similar experiments are performed in these same systems under a variety of non-reducing conditions, there are minimal changes in the apparent molecular weight of both the beta 1- and beta 2-adrenergic receptor binding subunits and no specifically labeled higher molecular weight proteins are observed suggesting that there are no disulfide linked subunits in mammalian beta-adrenergic receptors.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
31
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pubmed:volume |
116
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
777-82
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6316962-Animals,
pubmed-meshheading:6316962-Cricetinae,
pubmed-meshheading:6316962-Erythrocyte Membrane,
pubmed-meshheading:6316962-Lung,
pubmed-meshheading:6316962-Macromolecular Substances,
pubmed-meshheading:6316962-Mercaptoethanol,
pubmed-meshheading:6316962-Molecular Weight,
pubmed-meshheading:6316962-Myocardium,
pubmed-meshheading:6316962-Rats,
pubmed-meshheading:6316962-Receptors, Adrenergic, beta,
pubmed-meshheading:6316962-Swine
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pubmed:year |
1983
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pubmed:articleTitle |
The effect of reducing agents on the structure of mammalian beta-adrenergic receptors.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|