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Some properties of a purinergic receptor solubilized from human uterus membranes
Author(s) -
Ronca-Testoni S.,
Galbani P.,
Gambacciani M.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81152-7
Subject(s) - purinergic receptor , adenosine receptor , chemistry , receptor , adenosine , radioligand , membrane , ligand (biochemistry) , digitonin , biochemistry , centrifugation , myometrium , binding site , biophysics , biology , endocrinology , agonist , uterus
A purinergic receptor was identified in human myometrium membranes using 5'‐ N ‐[ 3 H]ethylcarboxamideadenosine ([ 3 H]NECA) as radioligand. Scatchard analysis of the binding data gave a K d of 123 nM with 2.3pmol ligand protein. Displacement studies indicated that the binding site had the characteristics of the A 2 adenosine receptors and some of those of the P 2 purinoceptors since it was inhibited by two slowly degradable ATP derivatives with IC 50 values comparable to that of NECA. The receptor was solubilized with sodium cholate and its binding properties were the same as those of the membrane‐bound form. No ‐SH group appeared to be essential for the binding activity. By density gradient centrifugation the purinergic receptor‐detergent complex was estimated to have an apparent molecular mass of 95 kDa.