Abstract:
:Opioid receptor binding properties of [3H]Tyr-D-Ala-Phe-Phe-NH2 (TAPP) were characterized in rat brain and Chinese hamster ovary (CHO) cells expressing the rat mu-receptor. In rat brain, [3H]TAPP labeled a single class of opioid sites with a dissociation constant (Kd) of 0.31 nM and maximal number of binding sites (Bmax) of 119 fmol/mg protein. In CHO-mu/1 cell membranes, the Kd and Bmax values were 0.78 nM and 1806 fmol/mg protein, respectively. Binding to rat brain was demonstrated to be pharmacologically identical to that obtained with CHO-mu/1 cell membranes and modulated by Na+ ions and guanine nucleotides. The high affinity and selectivity of [3H]TAPP together with its low non-specific binding make this radioligand a useful tool for labeling the native and cloned mu-opioid receptor.
journal_name
Peptidesjournal_title
Peptidesauthors
Spetea M,Otvös F,Tóth G,Nguyen TM,Schiller PW,Vogel Z,Borsodi Adoi
10.1016/s0196-9781(98)00023-0subject
Has Abstractpub_date
1998-01-01 00:00:00pages
1091-8issue
6eissn
0196-9781issn
1873-5169pii
S0196-9781(98)00023-0journal_volume
19pub_type
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