Binding of the estradiol-receptor complex to reconstituted nucleoacidic protein from calf uterus |
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Authors: | Patrick Ross Thomas S Ruh |
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Institution: | Department of Physiology, St. Louis University Medical School, St. Louis, MO U.S.A. |
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Abstract: | Non-histone protein-DNA complexes with acceptor activity for estradiol-receptor complexes were reconstituted from fractionated calf uterine chromatin. Acceptor activity had tissue specificity with target tissue binding exceeding non-target tissue binding. The binding of estradiol-receptor complexes to acceptor sites was dependent on intact non-histone protein-DNA complexes, reconstituted select non-histone proteins, and protein equivalent: DNA reconstitution ratios. 3H]Estradiol-receptor complexes were bound to reconstituted non-histone protein-DNA complexes (i.e., nucleoacidic protein) with a high affinity and with a limited number of binding sites. Fractionation of uterine chromatin non-histone proteins identified two major sets of non-histone proteins which had acceptor activity when reconstituted with DNA. Thus, it seems possible to reconstitute nucleoacidic protein fractions with specific acceptor activity for the calf uterine estrogen receptor. |
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Keywords: | Estrogen receptor Chromatin reconstitution Acceptor activity Non-histone protein Tissue specificity (Calf) Gdn·HCl guanidine hydrochloride PMSF phenylmethylsulfonyl fluoride |
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