Biomaterial Database

A1 adenosine receptors can occur manifesting two kinetic components of 8-cyclopentyl-1,3-[3H]dipropylxanthine ([3H]DPCPX) binding. 1994

V Casadó, and J Mallol, and R Franco, and C Lluis, and E I Canela

Departament de Bioquímica i Fisiologia, Facultat de Química, Universitat de Barcelona, Catalonia, Spain.

The results described in this paper show, for the first time, that A1 adenosine receptors can have two kinetic components for the binding of the antagonist [3H]DPCPX. At low ionic strength (< or = 42 mmol/l), dissociation of [3H]DPCPX bound to A1 receptors fitted better to a two kinetic components model than to a one kinetic component model. The kinetic constants were consistent with comparable Kd values for the two components of the antagonist binding, and therefore these two components cannot be distinguished by saturation isotherm analysis.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D001921	Brain	The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.	Encephalon
D002462	Cell Membrane	The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.	Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013552	Swine	Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).	Phacochoerus,Pigs,Suidae,Warthogs,Wart Hogs,Hog, Wart,Hogs, Wart,Wart Hog
D014970	Xanthines	Purine bases found in body tissues and fluids and in some plants.
D058915	Purinergic P1 Receptor Antagonists	Compounds that bind to and block the stimulation of PURINERGIC P1 RECEPTORS.	Adenosine Receptor Antagonist,P1 Purinoceptor Antagonist,Purinergic P1 Receptor Antagonist,Adenosine Receptor Antagonists,P1 Purinoceptor Antagonists,Antagonist, Adenosine Receptor,Antagonist, P1 Purinoceptor,Antagonists, Adenosine Receptor,Antagonists, P1 Purinoceptor,Purinoceptor Antagonist, P1,Purinoceptor Antagonists, P1,Receptor Antagonist, Adenosine,Receptor Antagonists, Adenosine
D018047	Receptors, Purinergic P1	A class of cell surface receptors that prefer ADENOSINE to other endogenous PURINES. Purinergic P1 receptors are widespread in the body including the cardiovascular, respiratory, immune, and nervous systems. There are at least two pharmacologically distinguishable types (A1 and A2, or Ri and Ra).	Adenosine Receptors,P1 Purinoceptors,Purinergic P1 Receptors,Receptors, Adenosine,Adenosine Receptor,P1 Purinoceptor,Receptor, Purinergic P1,P1 Receptor, Purinergic,P1 Receptors, Purinergic,Purinergic P1 Receptor,Purinoceptor, P1,Purinoceptors, P1,Receptor, Adenosine