Corresponding normalized mean binding values of Cav3.2 on calnexin in NEC (black bar) and GAERS brains (red bar).
Cui, Q. & Elstner, M. Density functional tight binding: values of semi-empirical methods in an ab initio era.
Since the gerbil NK1 receptor binding values were similar for all five compounds, differences in pharmacokinetics and brain penetration most likely account for the rank order.
(D) Corresponding mean binding values of CNXBD-mCherry on hIII-IVWT (black bar) and on hIII-IVR1573P (GAEred red bar) and hIII-IVT1606M (green bar) variants (n = 7).
LFS did not modify α1 receptor and adenylyl cyclase binding values.
(C) Corresponding mean binding values of CNXBD-mCherry on rCav3.2 WT- (black bar) and GAERS-III-IV linker (red bar) containing exon 25, and on WT- (green bar) and GAERS-III-IV linker (blue bar) lacking of the exon 25.
Plasma protein binding values obtained for 10 diverse compounds using standard dialysis equipment and the 96-well dialysis block validates this method.
Further, radioligand binding values calculated from these measurements were found to be more precise than those calculated from measurements obtained with manually drawn regions of interest (ROIs).
High quality epitope maps were achieved by performing the assays at concentrations of soluble SA antibody fusions and antibodies that were equivalent to their KD binding values for the hCXCL1WT (2.5 nM for SA129, 100 nM for SA138, 1.5 μM for SA157*, 0.1 nM for Ab275, and 0.25 nM for Ab276).
The HSA binding values were derived from the gradient retention times that were converted to the logarithm of the equilibrium constants (logK HSA) using data from a calibration set of molecules.
Concerning μ receptors, LFS decreased binding values in ipsilateral sensorimotor (7.2%) and temporal (5.6%) cortices, dentate gyrus (5.8% ipsi and 6.8% contralateral, respectively), and contralateral CA1 area of dorsal hippocampus (5.5%).
