[Binding of triiodothyronine to the nuclear matrix of the rat liver. The effect of thyroid hormones on the phosphorylation of nuclear matrix proteins].
The interaction of thyroid hormones with rat liver nuclear matrix proteins was studied. It was shown that the nuclear matrix contains the sites which bind triiodothyronine with a high affinity (Ka = 1.07 X 10(9) M-1) and limited capacity (maximal binding capacity--28.5 fmol triiodothyronine/100 micrograms protein). Electrophoretic analysis of triiodothyronine-binding matrix proteins revealed that the molecular mass of the major triiodothyronine-binding fraction is 50 000-52 000 Da. Injections of triiodothyronine to thyroidectomized animals stimulated the phosphorylation of all protein fractions of the nuclear matrix.
D000818:Animals; D034961:Antigens, Nuclear; D001667:Binding, Competitive; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008297:Male; D009698:Nucleoproteins / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats; D013965:Thyroidectomy; D013974:Thyroxine / Q000378:metabolism / Q000494:pharmacology; D014284:Triiodothyronine / Q000378:metabolism* / Q000494:pharmacology
D034961:Antigens, Nuclear; D009698:Nucleoproteins; D014284:Triiodothyronine; D013974:Thyroxine
Sviazyvanie triiodotironina s iadernym matriksom pecheni krys. Vliianie tireoidnykh gormonov na fosforilirovanie belkov iadernogo matriksa.