Temperature dependence of [3H]PAF binding to washed human platelets.
Our results indicate that the binding of [3H]PAF to a single class of high affinity sites on human platelets is endothermic and largely entropy-driven. The increase in entropy can be attributed to the disorganization of water molecules bound to both receptor and ligand during the binding process.
Borea
P A
PA
Istituto di Farmacologia, Università di Ferrara, Italy.
Montesi
L
L
Muzzolini
A
A
Fantozzi
R
R
D001792:Blood Platelets / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D010972:Platelet Activating Factor / Q000378:metabolism*; D010980:Platelet Membrane Glycoproteins; D011956:Receptors, Cell Surface / Q000032:analysis*; D043562:Receptors, G-Protein-Coupled; D013696:Temperature; D013816:Thermodynamics
D010972:Platelet Activating Factor; D010980:Platelet Membrane Glycoproteins; D011956:Receptors, Cell Surface; D043562:Receptors, G-Protein-Coupled; C039351:platelet activating factor receptor