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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1989-8-14
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pubmed:abstractText |
We have shown that delipidated rhodopsin immobilized on Concanavalin A-Sepharose is capable of binding transducin from crude bovine rod outer segment proteins and GIP-binding proteins (G proteins) of Go/Gi-type from solubilized bovine brain membrane as well. The binding is reversible in the presence of a solution containing 1.2% octyl-beta, D-glucopyranoside and 1 mM GTP. Also, alpha-subunits account for a large fraction of the G proteins which are bound to and then eluted from the immobilized rhodopsin. Concanavalin A-bound delipidated rhodopsin seems to be a useful model in isolating and purifying different G-proteins from crude cell lysates and solubilized membranes as well as for studying G-protein-receptor interaction.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
162
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
544-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2502113-Animals,
pubmed-meshheading:2502113-Binding Sites,
pubmed-meshheading:2502113-Cattle,
pubmed-meshheading:2502113-Chromatography, Ion Exchange,
pubmed-meshheading:2502113-GTP-Binding Proteins,
pubmed-meshheading:2502113-Lipid Metabolism,
pubmed-meshheading:2502113-Retinal Pigments,
pubmed-meshheading:2502113-Rhodopsin,
pubmed-meshheading:2502113-Rod Cell Outer Segment,
pubmed-meshheading:2502113-Transducin
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pubmed:year |
1989
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pubmed:articleTitle |
The binding of G proteins to immobilized delipidated rhodopsin.
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pubmed:affiliation |
Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
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pubmed:publicationType |
Journal Article
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