TABLE 1

125I-PYY saturation and competition binding in stably transfected CHO HAY1, HAY1T*, and HAY1S* clones

pKd and Bmax values were calculated from the direct fit to saturation experiments performed with 0.05 to 5.0 nM 125I-PYY, in which nonspecific binding was assessed with 1 μM BIBO3304. PYY, NPY, and BIBO3304 pIC50 values are given for competition assays performed with 10 pM radioligand; 1 μM GTPγS attenuated total 125I-PYY binding (expressed as percentage inhibition of total binding) without altering the pIC50 values for competing PYY significantly (range, 9.22-9.57). Data are expressed as mean ± S.E.M. from the number of experiments indicated in parentheses.

125I-PYY Saturation 125I-PYY Competition
pKdBmax pIC50 Inhibition by 1 μM GTPγS
PYY NPY BIBO3304
pmol/mg %
CHO-HAY1 9.52 ± 0.12 (5) 5.4 ± 1.6 (5) 9.52 ± 0.05 (7) 9.61 ± 0.09 (4) 9.32 ± 0.08 (4) 45.2 ± 4.1 (3)
CHO-HAY1S* 9.32 ± 0.07 (4) 5.5 ± 1.1 (4) 9.39 ± 0.04 (8) 9.80 ± 0.07 (5) 9.41 ± 0.07 (4) 49.8 ± 3.0 (3)
CHO-HAY1T* 9.48 ± 0.10 (5) 3.9 ± 1.1 (5) 9.85 ± 0.03 (6) 9.58 ± 0.05 (4) 9.48 ± 0.04 (3) 59.8 ± 0.9 (3)