| pubmed-article:208069 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:208069 | lifeskim:mentions | umls-concept:C0008356 | lld:lifeskim |
| pubmed-article:208069 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:208069 | lifeskim:mentions | umls-concept:C0001492 | lld:lifeskim |
| pubmed-article:208069 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
| pubmed-article:208069 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:208069 | lifeskim:mentions | umls-concept:C1511539 | lld:lifeskim |
| pubmed-article:208069 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:208069 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:208069 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:208069 | pubmed:dateCreated | 1978-9-1 | lld:pubmed |
| pubmed-article:208069 | pubmed:abstractText | Treatment of pigeon erythrocyte membranes with cholera toxin and NAD(+) enhanced the GTP stimulation and suppressed the F(-) activation of the adenylate cylase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1]. In the presence of NAD(+) labeled with (32)P in the AMP moiety the toxin catalyzed the covalent incorporation of radioactivity into membrane proteins with molecular weights (M(r)s) of 200,000, 86,000, and 42,000. Extraction of toxin-treated membranes with Lubrol PX followed by affinity chromatography on a GTP-Sepharose column resulted in a 200-fold purification of the 42,000-M(r) labeled protein and in its complete separation from the other labeled proteins. The fraction containing the purified GTP-binding component from toxin-treated membranes conferred an enhanced GTP-stimulated activity on adenylate cyclase solubilized from nontreated membranes. Likewise, the addition of GTP-binding fraction from nontreated membranes to an enzyme solubilized from toxin-treated membranes restored F(-) stimulation of the adenylate cyclase. The toxin-induced modification of adenylate cyclase and the incorporation of radioactivity into the 42,000-M(r) protein were partially reversed upon incubation with toxin and nicotinamide at pH 6.1. The results indicate that cholera toxin affects the adenylate cyclase system by catalyzing an ADP-ribosylation of the 42,000-M(r) component bearing the guanyl nucleotide regulatory site. | lld:pubmed |
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| pubmed-article:208069 | pubmed:language | eng | lld:pubmed |
| pubmed-article:208069 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:208069 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:208069 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:208069 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:208069 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:208069 | pubmed:author | pubmed-author:PfeufferTT | lld:pubmed |
| pubmed-article:208069 | pubmed:author | pubmed-author:CasselDD | lld:pubmed |
| pubmed-article:208069 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:208069 | pubmed:volume | 75 | lld:pubmed |
| pubmed-article:208069 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:208069 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:208069 | pubmed:pagination | 2669-73 | lld:pubmed |
| pubmed-article:208069 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:208069 | pubmed:year | 1978 | lld:pubmed |
| pubmed-article:208069 | pubmed:articleTitle | Mechanism of cholera toxin action: covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system. | lld:pubmed |
| pubmed-article:208069 | pubmed:publicationType | Journal Article | lld:pubmed |
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