pubmed-article:6436438 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6436438 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:6436438 | lifeskim:mentions | umls-concept:C1882598 | lld:lifeskim |
pubmed-article:6436438 | lifeskim:mentions | umls-concept:C0001492 | lld:lifeskim |
pubmed-article:6436438 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
pubmed-article:6436438 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:6436438 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:6436438 | pubmed:dateCreated | 1984-11-26 | lld:pubmed |
pubmed-article:6436438 | pubmed:abstractText | Five GTP binding proteins in rat cerebral cortex synaptic membranes were identified by photoaffinity labelling with [3H] or [32P](P3-azido-anilido)-P1-5' GTP (AAGTP). When AAGTP-treated membranes were incubated with colchicine or vinblastine and subsequently washed, a single AAGTP-labelled protein of 42 kD was released into the supernatant. About 30% of the total labelled 42-kD protein was released into supernatants from membranes pretreated with colchicine or vinblastine compared with 15% released from control membranes. The amount of adenylate cyclase regulatory subunit (G unit) remaining in these membranes was assessed with reconstitution studies after inactivating the adenylate cyclase catalytic moiety with N-ethylmaleimide (NEM). Forty to fifty percent of functional G units were lost from membranes treated with colchicine prior to washing. This 40-50% loss of functional G unit after colchicine treatment corresponds to the previously observed 42% loss of NaF and guanylyl-5'-imidodiphosphate [Gpp(NH)p]-activated adenylate cyclase. Release of the AAGTP-labelled 42-kD protein from colchicine-treated synaptic membranes is double that from lumicolchicine-treated membranes. This colchicine-mediated release of 42-kD protein correlates with a doubling of functional G unit released from synaptic membranes after colchicine treatment. These findings suggest multiple populations of the G unit within the synaptic plasma membrane, some of which may interact with cytoskeletal components. | lld:pubmed |
pubmed-article:6436438 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6436438 | pubmed:language | eng | lld:pubmed |
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pubmed-article:6436438 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:6436438 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6436438 | pubmed:month | Nov | lld:pubmed |
pubmed-article:6436438 | pubmed:issn | 0022-3042 | lld:pubmed |
pubmed-article:6436438 | pubmed:author | pubmed-author:BitenskyM WMW | lld:pubmed |
pubmed-article:6436438 | pubmed:author | pubmed-author:WheelerG LGL | lld:pubmed |
pubmed-article:6436438 | pubmed:author | pubmed-author:SteinP JPJ | lld:pubmed |
pubmed-article:6436438 | pubmed:author | pubmed-author:RasenickM MMM | lld:pubmed |
pubmed-article:6436438 | pubmed:author | pubmed-author:KosackC MCM | lld:pubmed |
pubmed-article:6436438 | pubmed:author | pubmed-author:MalinaR LRL | lld:pubmed |
pubmed-article:6436438 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6436438 | pubmed:volume | 43 | lld:pubmed |
pubmed-article:6436438 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6436438 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6436438 | pubmed:pagination | 1447-54 | lld:pubmed |
pubmed-article:6436438 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:6436438 | pubmed:year | 1984 | lld:pubmed |
pubmed-article:6436438 | pubmed:articleTitle | Photoaffinity identification of colchicine-solubilized regulatory subunit from rat brain adenylate cyclase. | lld:pubmed |
pubmed-article:6436438 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:6436438 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:6436438 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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