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Atypical [ 3 H]Clonidine Binding Sites in Human Caudate and Platelets on Cryostat‐cut Sections
Author(s) -
ZHU H,
HALARIS A,
PILETZ JE
Publication year - 2003
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1304.038
Subject(s) - chemistry , imidazoline receptor , platelet , clonidine , binding site , affinities , human blood , filtration (mathematics) , biophysics , stereochemistry , biochemistry , medicine , endocrinology , biology , physiology , statistics , mathematics
A bstract : Pharmacological characterization is described for a human imidazoline binding site (I‐site) labeled by [ 3 H]clonidine using standard autoradiographic method. Under conditions that mask a 2 ‐adrenergic sites, only a single high affinity site was observed in human caudate and blood platelet sections. Affinity constants (K i ) were highly correlated between the two tissues ( r 5 0.90, P 5 0.0003). This site is dissimilar to classical I 1 and I 2 sites, even though both tissues possess abundant I 1 and I 2 sites by filtration binding methods. It is suggested that the isotonic buffer conditions inherent to the procedure alter drug affinities to the classical I 1 site.