[A study of the interaction of immobilized delipidized rhodopsin with G-proteins].
It was shown that delipidated rhodopsin immobilized on concanavalin A-Sepharose (Rimm) binds with high selectivity transducin from total extracts of rod outer segment protein as well as the regulatory GTP-binding Gi- and Go-like proteins from solubilized membranes of bovine brain. The Rimm-bound proteins are eluted in the presence of the nonionic detergent, octyl glucoside, and GTP. This suggests that Rimm can be used as an affinity adsorbent for the isolation and purification of G-proteins.
Dizhur
A M
AM
Nekrasova
E R
ER
Filippov
P P
PP
D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D003208:Concanavalin A; D004591:Electrophoresis, Polyacrylamide Gel; D019204:GTP-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*; D050356:Lipid Metabolism; D012168:Retinal Pigments / Q000378:metabolism*; D012243:Rhodopsin / Q000378:metabolism*; D012374:Rod Cell Outer Segment / Q000378:metabolism; D015293:Transducin / Q000378:metabolism
D012168:Retinal Pigments; D003208:Concanavalin A; D012243:Rhodopsin; D019204:GTP-Binding Proteins; D015293:Transducin
Izuchenie vzaimodeĭstviia immobilizovannogo delipidizirovannogo rodopsina s G-belkami.