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Sethy VH, Mccall JM. 
“High-Affinity (3H)-Dexoxadrol Binding to Rat Brain Membranes”. 
Drug Development Research. 1984;4:635-645.
Specific binding of (3H)-dexoxadrol to rat brain membrane was saturable. The specific binding represented 74 to 820f total binding. Scatchard analysis of the data demonstrated the existence of high and low-affinity binding sites. The kinetic constants for the corresponding binding sites were as follows: Kd' = 1.68 nM, Bmax' =0.4 pmol/mg protein, Kdz = 26.1 nM, and Bmax2 - 3.t pmol/mg protein. Binding reached equilibrium within 5 minutes of incubation at 25 degrees C. Optimum binding was observed between:the pH range of 7.4 to 9. Binding was dependent on protein concentration and was reduced by denaturation of protein and by proteolytic enzyme. (3H)-dexoxadrol binding was inhibited by drugs pharmacologically similar to phencyclidine (POP) and bound (3H)-dexoxedrol could be rapidly displaced by cold PCP.
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