| pubmed-article:2187531 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2187531 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:2187531 | lifeskim:mentions | umls-concept:C0035499 | lld:lifeskim |
| pubmed-article:2187531 | lifeskim:mentions | umls-concept:C0018328 | lld:lifeskim |
| pubmed-article:2187531 | lifeskim:mentions | umls-concept:C0040663 | lld:lifeskim |
| pubmed-article:2187531 | lifeskim:mentions | umls-concept:C1521970 | lld:lifeskim |
| pubmed-article:2187531 | lifeskim:mentions | umls-concept:C1148916 | lld:lifeskim |
| pubmed-article:2187531 | lifeskim:mentions | umls-concept:C0678640 | lld:lifeskim |
| pubmed-article:2187531 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
| pubmed-article:2187531 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:2187531 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:2187531 | pubmed:dateCreated | 1990-6-26 | lld:pubmed |
| pubmed-article:2187531 | pubmed:abstractText | Transducin (Gt) is a member of a family of receptor-coupled signal-transducing guanine nucleotide (GN) binding proteins (G-proteins). Light-activated rhodopsin is known to catalyze GN exchange on Gt, resulting in the formation of the active state of the Gt alpha-GTP complex. However, purified preparations of Gt have been shown to exchange GN in the absence of activated receptors [Wessling-Resnick, M., & Johnson, G. L. (1987) Biochemistry 26, 4316-4323]. To evaluate the role of rhodopsin in the activation of Gt, we studied GN-binding characteristics of different preparations of Gt. Gt preparations obtained rom the supernate of GTP-treated bovine rod outer segment (ROS) disks, followed by removal of free GTP on a Sephadex G-25 column, bound GTP gamma S at 30 degrees C in the absence of added exogenous rhodopsin with an activity of 1 mol of GTP gamma S bound/mol of Gt (Gt-I preparations). Binding of GTP gamma S to Gt-I preparations closely correlated with the activation of ROS disk cGMP phosphodiesterase. GN-binding activity of Gt-I preparations was dependent on reaction temperature, and no binding was observed at 4 degrees C. In the presence of 10 microM bleached rhodopsin, Gt-I preparations bound GTP gamma S at 4 degrees C. However, hexylagarose chromatography of Gt-I preparations led to a preparation of Gt that showed less than 0.1 mol/mol binding activity following 60-min incubation at 30 degrees C in the absence of rhodopsin (Gt-II preparations).(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
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| pubmed-article:2187531 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2187531 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2187531 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2187531 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2187531 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2187531 | pubmed:author | pubmed-author:NorthupJ KJK | lld:pubmed |
| pubmed-article:2187531 | pubmed:author | pubmed-author:FawziA BAB | lld:pubmed |
| pubmed-article:2187531 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2187531 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:2187531 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:2187531 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2187531 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2187531 | pubmed:pagination | 3804-12 | lld:pubmed |
| pubmed-article:2187531 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:2187531 | pubmed:meshHeading | pubmed-meshheading:2187531-... | lld:pubmed |
| pubmed-article:2187531 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2187531 | pubmed:articleTitle | Guanine nucleotide binding characteristics of transducin: essential role of rhodopsin for rapid exchange of guanine nucleotides. | lld:pubmed |
| pubmed-article:2187531 | pubmed:affiliation | Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06510. | lld:pubmed |
| pubmed-article:2187531 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2187531 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2187531 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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