Effect of GTP on the rhodopsin-G-protein complex by transient formation of extra metarhodopsin II.
Biochim Biophys Acta
; 810(2): 278-81, 1985 Nov 27.
Article
em En
| MEDLINE
| ID: mdl-3933561
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Pigmentos da Retina
/
Rodopsina
/
Proteínas de Ligação ao GTP
/
Guanosina Trifosfato
Limite:
Animals
Idioma:
En
Ano de publicação:
1985
Tipo de documento:
Article