Identificador persistente para citar o vincular este elemento: http://hdl.handle.net/10553/44456
Título: Characterization of diadenosine tetraphosphate (Ap<inf>4</inf>A) binding sites in cultured chromaffin cells: evidence for a P<inf>2y</inf>site
Autores/as: Pintor, Jesús
Torres, Magdalena
Castro López-Tarruella, Enrique 
Miras‐Portugal, M. Teresa
Clasificación UNESCO: 32 Ciencias médicas
Fecha de publicación: 1991
Editor/a: 0007-1188
Publicación seriada: British journal of pharmacology 
Resumen: Diadenosine tetraphosphate (Ap4A) a dinucleotide, which is stored in secretory granules, presents two types of high affinity binding sites in chromaffin cells. A Kd value of 8 +/- 0.65 x 10(-11) M and Bmax value of 5420 +/- 450 sites per cell were obtained for the high affinity binding site. A Kd value of 5.6 +/- 0.53 x 10(-9) M and a Bmax value close to 70,000 sites per cell were obtained for the second binding site with high affinity. 2. The diadenosine polyphosphates, Ap3A, Ap4A, Ap5A and Ap6A, displaced [3H]-Ap4A from the two binding sites, the Ki values being 1.0 nM, 0.013 nM, 0.013 nM and 0.013 nM for the very high affinity binding site and 0.5 microM, 0.13 microM, 0.062 microM and 0.75 microM for the second binding site. 3. The ATP analogues displaced [3H]-Ap4A with the potency order of the P2y receptors, adenosine 5'-O-(2 thiodiphosphate) (ADP-beta-S) greater than 5'-adenylyl imidodiphosphate (AMP-PNP) greater than alpha, beta-methylene ATP (alpha, beta-MeATP), in both binding sites. The Ki values were respectively 0.075 nM, 0.2 nM and 0.75 nM for the very high affinity binding site and 0.125 microM, 0.5 microM and 0.9 microM for the second binding site.
URI: http://hdl.handle.net/10553/44456
ISSN: 0007-1188
DOI: 10.1111/j.1476-5381.1991.tb12363.x
Fuente: British Journal of Pharmacology [ISSN 0007-1188], v. 103, p. 1980-1984
Colección:Artículos
Vista completa

Google ScholarTM

Verifica

Altmetric


Comparte



Exporta metadatos



Los elementos en ULPGC accedaCRIS están protegidos por derechos de autor con todos los derechos reservados, a menos que se indique lo contrario.