High affinity specific antiestrogen binding sites are concentrated in rough microsomal membranes of rat liver.
Saturation and competitive binding analyses demonstrated the presence of a high affinity (KD = 0.92 nM), specific antiestrogen binding site (AEBS) in rat liver microsomes and at least 75% of total liver AEBS was recovered in this fraction. When microsomes were further separated into smooth and rough fractions, AEBS was concentrated in the latter. Subsequent dissociation of ribosomes from the rough membranes revealed that AEBS was associated with the membrane and not the ribosomal fraction. Antiestrogen binding activity could not be extracted from membranes with 1 M KCl or 0.5 M acetic acid but could be solubilized with sodium cholate. These data indicate that AEBS is an integral membrane component of the rough microsomal fraction of rat liver.
D000818:Animals; D001667:Binding, Competitive; D005260:Female; D007425:Intracellular Membranes / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D008862:Microsomes, Liver / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D011955:Receptors, Drug; D011960:Receptors, Estrogen / Q000302:isolation & purification / Q000378:metabolism*; D012995:Solubility; D013347:Subcellular Fractions / Q000378:metabolism
D011955:Receptors, Drug; D011960:Receptors, Estrogen