Occurrence of protein kinases NI and NII in human and porcine thyroids.
Cyclic nucleotide-independent protein kinases that preferentially phosphorylated casein and phosvitin as substrate were detected in the nuclei of human and porcine thyroid tissues, and compared with those from rat liver. Enzymes were extracted from the isolated nuclei with a buffer solution containing 0.4 M NaCl, and analyzed by DEAE-Sephadex and phosphocellulose column chromatographies. The chromatographies, together with the characterization of the enzymes, demonstrated that human and porcine thyroid tissues contained two major casein kinases in the cell nuclei, the properties of which revealed that they are to be identified as protein kinases NI and NII.
D000818:Animals; D002413:Cations, Divalent / Q000494:pharmacology; D002467:Cell Nucleus / Q000201:enzymology; D002482:Cellulose / Q000031:analogs & derivatives; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D006493:Heparin / Q000494:pharmacology; D006801:Humans; D008099:Liver / Q000201:enzymology; D008297:Male; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity; D013552:Swine; D013961:Thyroid Gland / Q000201:enzymology*
D002413:Cations, Divalent; D002482:Cellulose; D006493:Heparin; C008881:phosphocellulose; D011494:Protein Kinases; C036749:protein kinase NI; C026813:protein kinase NII