Abstract
The phenomenon of steroid-protein interaction has been examined in terms of ultraviolet difference spectra. In the case of interactions of serum albumins and some α,β-unsaturated ketosteroids two spectral effects are discernible, one attributed to the perturbation of the steroid absorption band by a hydrophobic environment at a binding site and the other to perturbation of aromatic amino acid bands. Interaction with androstenolone, which does not have the α,β-unsaturated ketone group, reveals difference troughs at approximately 235, 282, and 288 mμ which have been attributed to a red shift of aromatic absorption bands. Interaction of steroids with several enzyme proteins exhibits, under the conditions used, poorly defined difference spectra which are unlike the ones for serum albumins.
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