Parathyroid Hormone Receptors of Renal Cortex: Specific Binding of Biologically Active, 125I-Labeled Hormone and Relationship to Adenylate Cyclase Activation
AUTOR(ES)
Di Bella, Francis P.
RESUMO
Biologically active 125I-labeled bovine parathyroid hormone (prepared by electrolytic iodination) and its synthetic NH2-terminal (1-34) biologically active fragment bound rapidly and specifically to a purified plasma membrane preparation from bovine renal cortex. Binding of labeled intact hormone or labeled NH2-terminal (1-34) peptide was inhibited competitively by unlabeled (1-34) peptide in the same range of concentrations that activated renal cortical 3′:5′-adenylate cyclase (EC 4.6.1.1) in these membranes. The concentrations of synthetic (1-34) peptide for half-maximal inhibition of binding of labeled hormone as well as half-maximal activation of the enzyme were about 0.6 μM (2.5 μg/ml). Therefore it is likely that the binding activity studied represents a physiologically important renal receptor for parathyroid hormone.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=388085Documentos Relacionados
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