Journal article
The binding of G proteins to immobilized delipidated rhodopsin
Biochemical and biophysical research communications, v 162(1), pp 544-549
14 Jul 1989
PMID: 2502113
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Abstract
We have shown that delipidated rhodopsin immobilized on Concanavalin A-Sepharose is capable of binding transducin from crude bovine rod outer segment proteins and GTP-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-β,D-glucopyranoside and 1 mM GTP. Also, alfa-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 lyzates and solubilized membranes as well as for studying G-protein — receptor interaction.
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Details
- Title
- The binding of G proteins to immobilized delipidated rhodopsin
- Creators
- Alexander M. Dizhoor - Lomonosov Moscow State UniversityElina R. Nekrasova - Lomonosov Moscow State UniversityPavel P. Philippov - Lomonosov Moscow State University
- Publication Details
- Biochemical and biophysical research communications, v 162(1), pp 544-549
- Publisher
- Elsevier Inc
- Number of pages
- 6
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Neurobiology and Anatomy
- Web of Science ID
- WOS:A1989AE88500079
- Scopus ID
- 2-s2.0-0024344359
- Other Identifier
- 991022035112404721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics