Some properties of a purinergic receptor solubilized from human uterus membranes

FEBS Letters

Gambacciani, M.¹  Ronca-Testoni, S.¹  Galbani, P.¹ 

[1] Institute of Biological Chemistry and Institute of Obstetrics and Gynaecology, School of Medicine, University of Pisa, 56100 Pisa, Italy

关键词: Purinergic receptor5'-N-Ethylcarboxamideadenosine;    Human uterus membrane;    Receptor solubilization;    L-PIA;    L-N 6-phenylisopropyladenosine;    CHA;    N 6-cyclohexyladenosine;    NECA;    5'-N-ethylcarboxamideadenosine;    NEM;    N-ethylmaleimide;    p-CMPS;    p-chloromercuriphenylsulfonic acid;   

DOI  :  10.1016/0014-5793(84)81152-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A purinergic receptor was identified in human myometrium membranes using 5'-N-[³H]ethylcarboxamideadenosine ([³H]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 A₂ adenosine receptors and some of those of the P₂ 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.

【 授权许可】

Unknown