The binding of G proteins to immobilized delipidated rhodopsin.
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.
Dizhoor
A M
AM
Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Nekrasova
E R
ER
Philippov
P P
PP
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002852:Chromatography, Ion Exchange; D019204:GTP-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*; D050356:Lipid Metabolism; D012168:Retinal Pigments / Q000378:metabolism*; D012243:Rhodopsin / Q000302:isolation & purification / Q000378:metabolism*; D012374:Rod Cell Outer Segment / Q000032:analysis; D015293:Transducin / Q000378:metabolism
D012168:Retinal Pigments; D012243:Rhodopsin; D019204:GTP-Binding Proteins; D015293:Transducin