[Molecular profile of the aminopherases of rat heart cytostructures induced by toxic doses of thyroxine].
The development of thyrotoxin intoxication is attended by a sharply increased activity of aminopherases localized in the nuclei, mitochondria and hyaloplasm. The molecular pattern of the study enzymes undergoes a substantial change and is supplemented with new isoforms in the cathod portion of the spectrum embracing the alanine-aminotranspherase of the nuclei and hyaloplasm, and that of the aspartate-aminotranspherase of the nuclei and mitochondria. Actinomycin D, an inhibitor of transcription, abolishes the effect of thyrotoxin stimulating the aminopherase activity and induction of the hormones of new molecular forms of the aminopherases.
D000410:Alanine Transaminase / Q000096:biosynthesis*; D000818:Animals; D001219:Aspartate Aminotransferases / Q000096:biosynthesis*; D002467:Cell Nucleus / Q000201:enzymology; D003609:Dactinomycin / Q000627:therapeutic use; D004790:Enzyme Induction; D007527:Isoenzymes / Q000096:biosynthesis*; D008297:Male; D008928:Mitochondria / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology* / Q000648:ultrastructure; D051381:Rats; D013974:Thyroxine / Q000037:antagonists & inhibitors / Q000506:poisoning*
D007527:Isoenzymes; D003609:Dactinomycin; D001219:Aspartate Aminotransferases; D000410:Alanine Transaminase; D013974:Thyroxine
Molekuliarynĭ profil' aminoferaz tsitostruktur serdtsa krys, indutsirovannykh toksiceskimi dozami tiroksina