The high‐affinity binding of the cGMP analogue 8‐(5‐thioacetamidofluorescein)‐cGMP to rod outer segment membranes depleted of peripherally bound proteins has been defined by equilibrium dialysis (mean ± SD): (a) membranes contain about one cGMP binding site per 130 rhodopsin molecules; (b) the concentration of free ligand for half saturation is 2.0 ± 0.6 μM; (c) the apparent Hill coefficient of the bound versus free ligand relationship is 1.7 ± 0.5; (d) half saturation of the binding sites is sufficient for 85% activation of calcium permeability. A gating mechanism is proposed. Copyright © 1985, Wiley Blackwell. All rights reserved
Binding stoichiometry of a fluorescent cGMP analogue to membranes of retinal rod outer segments / Caretta, A.; Cavaggioni, A.; Sorbi, R. T.. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - 153:1(1985), pp. 49-53. [10.1111/j.1432-1033.1985.tb09265.x]
Binding stoichiometry of a fluorescent cGMP analogue to membranes of retinal rod outer segments
CARETTA A.
Investigation
;CAVAGGIONI A.Funding Acquisition
;
1985-01-01
Abstract
The high‐affinity binding of the cGMP analogue 8‐(5‐thioacetamidofluorescein)‐cGMP to rod outer segment membranes depleted of peripherally bound proteins has been defined by equilibrium dialysis (mean ± SD): (a) membranes contain about one cGMP binding site per 130 rhodopsin molecules; (b) the concentration of free ligand for half saturation is 2.0 ± 0.6 μM; (c) the apparent Hill coefficient of the bound versus free ligand relationship is 1.7 ± 0.5; (d) half saturation of the binding sites is sufficient for 85% activation of calcium permeability. A gating mechanism is proposed. Copyright © 1985, Wiley Blackwell. All rights reservedI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
