Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c.
@article{Johnson1988PositiveEO, title={Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c.}, author={E. F. Johnson and G. Schwab and L. Vickery}, journal={The Journal of biological chemistry}, year={1988}, volume={263 33}, pages={ 17672-7 } }
The binding of the amino steroid, 22-amino-23,24-bisnor-5-cholen-3 beta-ol (22-ABC), to rabbit liver cytochrome P-450 3c was studied using purified P-450 3c and liver microsomes prepared from rifampicin-treated B/J rabbits. 22-ABC binds to purified cytochrome P-450 3c producing a type II spectral change reflecting the coordination of the amine with the heme iron of the protein. In the absence of allosteric effectors, the binding is characterized by a Ks of 5 microM. In the presence of alpha… CONTINUE READING
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