| pubmed-article:6386524 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6386524 | lifeskim:mentions | umls-concept:C0020731 | lld:lifeskim |
| pubmed-article:6386524 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:6386524 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:6386524 | lifeskim:mentions | umls-concept:C0206131 | lld:lifeskim |
| pubmed-article:6386524 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:6386524 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:6386524 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6386524 | pubmed:dateCreated | 1984-12-10 | lld:pubmed |
| pubmed-article:6386524 | 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. | lld:pubmed |
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| pubmed-article:6386524 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6386524 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6386524 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6386524 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:6386524 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:6386524 | pubmed:author | pubmed-author:MalbonC CCC | lld:pubmed |
| pubmed-article:6386524 | pubmed:author | pubmed-author:RapiejkoP JPJ | lld:pubmed |
| pubmed-article:6386524 | pubmed:author | pubmed-author:Garciá-SáinzJ... | lld:pubmed |
| pubmed-article:6386524 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6386524 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:6386524 | pubmed:volume | 176 | lld:pubmed |
| pubmed-article:6386524 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6386524 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6386524 | pubmed:pagination | 301-6 | lld:pubmed |
| pubmed-article:6386524 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:6386524 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6386524 | pubmed:articleTitle | Pertussis toxin catalyzes the ADP-ribosylation of two distinct peptides, 40 and 41 kDa, in rat fat cell membranes. | lld:pubmed |
| pubmed-article:6386524 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6386524 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6386524 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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