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Biochim Biophys Acta. 1985 Nov 27;810(2):278-81.

Effect of GTP on the rhodopsin-G-protein complex by transient formation of extra metarhodopsin II.


The light-induced transient interaction between rhodopsin and G-protein in the presence of GTP has been measured by the formation of extra metarhodopsin II. Disc membranes were recombined with the hypotonic extract containing the G-protein. Without GTP, a flash induces stable rhodopsin-G-protein complexes which dissociate upon addition of GTP. In low GTP (less than 10 microM) transient rhodopsin X G-protein interaction is observed. Rhodopsin X G-protein dissociates the faster, the more GTP is present (rate of dissociation, 0.3/s at 5 microM GTP; T = 3.5 degrees C). The results corroborate that the uptake of GTP terminates the rhodopsin-G-protein complex and allow an estimation of the rhodopsin X G-protein lifetime.

[Indexed for MEDLINE]

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