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Evidence that most high-affinity ATP binding sites on aortic endothelial cells and membranes do not correspond to P2 receptors.

par Motte, Serge ;Swillens, Stéphane ;Boeynaems, Jean-Marie
Référence European journal of pharmacology, 307, 2, page (201-209)
Publication Publié, 1996-06

Article révisé par les pairs

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Titre:	Evidence that most high-affinity ATP binding sites on aortic endothelial cells and membranes do not correspond to P2 receptors.
Auteur:	Motte, Serge; Swillens, Stéphane; Boeynaems, Jean-Marie
Informations sur la publication:	European journal of pharmacology, 307, 2, page (201-209)
Statut de publication:	Publié, 1996-06
Sujet CREF:	Sciences bio-médicales et agricoles
MeSH keywords:	Adenosine Diphosphate -- analogs & derivatives
	Adenosine Diphosphate -- pharmacology
	Adenosine Triphosphate -- analogs & derivatives
	Adenosine Triphosphate -- blood
	Adenosine Triphosphate -- metabolism
	Adenosine Triphosphate -- pharmacology
	Animals
	Aorta -- cytology
	Aorta -- metabolism
	Binding Sites
	Binding, Competitive
	Cattle
	Cell Membrane -- metabolism
	Cells, Cultured
	Cytidine Triphosphate -- pharmacology
	Endothelium -- cytology
	Endothelium -- metabolism
	Inositol Phosphates -- blood
	Inositol Phosphates -- metabolism
	Kinetics
	Models, Biological
	Osmolar Concentration
	Phosphorus Radioisotopes -- diagnostic use
	Protein Binding -- drug effects
	Receptors, Purinergic -- blood
	Receptors, Purinergic -- metabolism
	Receptors, Purinergic P2 -- blood
	Receptors, Purinergic P2 -- metabolism
	Sulfur Radioisotopes -- diagnostic use
	Uridine Diphosphate -- pharmacology
	Uridine Triphosphate -- blood
	Uridine Triphosphate -- metabolism
Note générale:	In Vitro
	Journal Article
	Research Support, Non-U.S. Gov't
Langue:	Anglais
Identificateurs:	urn:issn:0014-2999
	info:pii/0014-2999(96)00234-8
	info:pmid/8832222