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- W2433396325 abstract "its effect may be simply due to formation of phosphomolybdate complexes or by some other direct interaction in the oligonucleotide-binding site (see above). The dissociation rate constants for [3H]oestradiol from receptor in phosphate buffer at 29°C after l h of labelling at 4°C were k l 0.09+0.02min-l and k 2 3 .28k1 .56~ 10-3min-1 (meanks.D.;n= 12). Theproportion of receptor present as the slow-dissociating form was 21.6 & 5.5%. Neither this proportion, which was equivalent to the maximum proportion of receptor capable of binding to oligo(dT)-cellulose, nor the rate constants were altered by any of the procedures described above. Therefore appearance of the slow-dissociating form of receptor occurs before activation to a nucleotide-binding state, but appears to determine overall the extent of oligonucleotide binding. The amount of receptor with slow dissociation kinetics that can bind to a oligonucleotide can be regulated by changes in the receptor's oligonucleotide site involving dissociation of low-molecular-weight components, the presence of reduced thiol groups and possibly a phosphorylation/dephosphorylation mechanism. Molybdate may exert a plurality of effects when preventing receptor binding to oligo(dT)cellulose. Overall activation of receptor to a nucleotidebinding form involves two separate processes mediating changes in dissociation kinetics and exposure of the nucleotide-binding site." @default.
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- W2433396325 date "1984-04-01" @default.
- W2433396325 modified "2023-09-24" @default.
- W2433396325 title "The interaction of oestrogen receptor with oligodeoxynucleotides" @default.
- W2433396325 doi "https://doi.org/10.1042/bst0120322" @default.
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