. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. B — — 120 TIME (min) Figure 2. Time course of R-PIA-induced dissociation of specific [3H]CHA binding in Antimora rostrata brain membranes. Membranes ( mg protein) were first incubated at 5°C with nM ['H]CHA for 240 min to allow binding to reach equilibrium. Sixty pM R-PIA was added in a negligible volume (1% of the total incubation volume) to initiate the dissociation reaction. The nonspecific binding, which has been subtracted from each experimental point, was determined in the presence of 60 pM R-PIA.
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. B — — 120 TIME (min) Figure 2. Time course of R-PIA-induced dissociation of specific [3H]CHA binding in Antimora rostrata brain membranes. Membranes ( mg protein) were first incubated at 5°C with nM ['H]CHA for 240 min to allow binding to reach equilibrium. Sixty pM R-PIA was added in a negligible volume (1% of the total incubation volume) to initiate the dissociation reaction. The nonspecific binding, which has been subtracted from each experimental point, was determined in the presence of 60 pM R-PIA. Inset depicts the first-order replot of dissocia- tion data and represents the best least-squares regression line. Data shown are from a single experiment. determined in the presence of 30 nAf R-PIA, saturated over the range of to approximately 16 nA/. Non- specific binding increased linearly as a function of ['HI- GH A concentration. Analysis of the [3H]CH A saturation isotherm, using equations based on mass action princi- ples, indicated that the data were adequately described by interaction with a single high affinity state of the re- ceptor. Computer modeling of replicate experiments. 0 5 10 PH]CHA (nM) Figure 3. Equilibrium saturation binding of ['H]CHA \oAntimuru rostrata brain membranes at 5°C. Membranes were incubated 150 min with 11 concentrations of free ['H]CHA ranging from to nA/in this experiment. Specific binding is indicated by the filled circles. Nonspecific binding, shown by the open triangles, was determined in the presence of 30 iiM R-PIA. MR 1234567 1234567 Figure 4. Autoradiogram of teleost fish brain membrane prepara- tions [32P]ADP-nbosylated by pertussis toxin at 5°C. Preparations were incubated for 2 h with [32P]NAD with (A) or without (B) pertussis toxin. The samples were denatured and subjected to sodium dodecyl sulfatepolyacrylamideelectrophoresisin acrylamide gels follow- ing Laemmli (1970). The gels were dried and expo
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