Title : Binding of radiolabeled antagonist to platelet-activating-factor receptor in human lung membranes: shifting of agonist binding affinity states by cations and guanine nucleotide.

Pub. Date : 1990

PMID : 2154654






4 Functional Relationships(s)
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1 Binding of the radiolabeled platelet-activating-factor (PAF) receptor antagonist RP52770, [( 3H]-N-(3-chlorophenyl)-3-(3-pyridinyl)-1H, 3H-pyrrolo- [1,2-c]thiazole-7-carboxamide) to receptors in human lung membranes was time- dependent, protein-dependent, reversible and saturable. [( 3h]-n-(3-chlorophenyl)-3-(3-pyridinyl)-1h platelet activating factor receptor Homo sapiens
2 Binding of the radiolabeled platelet-activating-factor (PAF) receptor antagonist RP52770, [( 3H]-N-(3-chlorophenyl)-3-(3-pyridinyl)-1H, 3H-pyrrolo- [1,2-c]thiazole-7-carboxamide) to receptors in human lung membranes was time- dependent, protein-dependent, reversible and saturable. 3h-pyrrolo- [1,2-c]thiazole-7-carboxamide platelet activating factor receptor Homo sapiens
3 [3H]-RP52770 binding to the PAF receptor was competitively displaced by PAF and receptor antagonists. Tritium platelet activating factor receptor Homo sapiens
4 These results clearly demonstrate that cations and guanine nucleotide can regulate the affinity states of the PAF receptor in human lung membranes. Guanine Nucleotides platelet activating factor receptor Homo sapiens