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1 receptor (K(d) = 0.54 nm) with a curvilinear Scatchard plot.
2 mined by recasting the data in the form of a Scatchard plot.
3 rface EGF-binding sites inferred from curved Scatchard plots.
4 as wild type and also displayed curvilinear Scatchard plots.
5 can be very important in analyzing data from Scatchard plots.
7 elation to varying concentrations of GlcNAc, Scatchard plot analysis and competitive inhibition with
8 escence double-staining, ligand binding, and Scatchard plot analysis demonstrated that mEar1 bound to
21 inding sites were identified in rat aorta by Scatchard plot analysis with a Kd of 0.25+/-0.07 nM and
22 ng in varying concentrations of the peptide, Scatchard plot analysis, and competitive inhibition with
23 NA was obtained from the negative slope of a Scatchard plot and a comparison of the binding constants
24 onic acid that was defined by a curved Eadie-Scatchard plot and a Hill coefficient of 1.36 +/- 0.05.
25 coefficient of 1.29 +/- 0.06, a curved Eadie-Scatchard plot, and activation by low concentrations of
26 omewhat higher than those estimated from the Scatchard plot because of concentration dependence, but
28 EGFR extracellular region, we show here how Scatchard plot curvature arises from negatively cooperat
29 od that does not have the limitations of the Scatchard plot for analysis of amphitropic proteins was
30 ngly cooperative ACTD binding and the curved Scatchard plot for the self-complementary d(CGTCGACG) ma
35 (3-hydroxybenzyl)hydrazine, as indicated by Scatchard plots, or with 3-hydrazinopropionate, as shown
37 in the characteristic concave-up curvilinear Scatchard plots seen when EGF binding to intact EGFR is
40 ion procedure was used in conjunction with a Scatchard plot to study the binding of the methylphenazi
43 wild-type EGF receptor showed a curvilinear Scatchard plot with both high- and low-affinity forms of