Abstract
Summary Two classes of phorbol ester binding sites have been demonstrated in the nuclear fraction of liver from female CD-1 mice. Equilibrium binding studies of 0.40 M NaCl nuclear extracts yielded a sigmoidal saturation curve which was resolved by Hill plot analysis into two components. However, when nuclei were extracted in 0.24 M NaCl, the 12-0-tetradecanoylphorbol-13-acetate saturation curve of the extract was biphasic in shape consisting of both high and low affinity binding sites termed Class I and II receptors. When the 0.24 M NaCl extracted nuclear pellet was extracted further in 0.40 M NaCl, saturation analysis of the extract revealed only the low affinity binding site (Class II). This is the first study to identify the existence of phorbol ester receptors in liver nuclei.
Published Version
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