Phosphorylation of purified Novikoff hepatoma topoisomerase I

The purified Novikoff hepatoma nuclear phosphoprotein with a molecular weight of 110 kdalton and pI 8.4 was found to be a type I topoisomerase. When isolated from 32P-labeled Novikoff ascites cells or incubated in vitro with protein kinase, phosphoserine was found to be its major phosphorylated amin...

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Veröffentlicht in:	Biochemical and biophysical research communications 1983-03, Vol.111 (3), p.897-905
Hauptverfasser:	Durban, Egon, Mills, John S., Roll, David, Busch, Harris
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkaline Phosphatase - metabolism Animals DNA topoisomerase I DNA Topoisomerases, Type I - isolation & purification DNA Topoisomerases, Type I - metabolism Enzyme Activation hepatoma Liver Neoplasms, Experimental - enzymology Neoplasm Proteins - isolation & purification Phosphorylation Protein Kinases - metabolism Rats
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Beschreibung
Zusammenfassung:	The purified Novikoff hepatoma nuclear phosphoprotein with a molecular weight of 110 kdalton and pI 8.4 was found to be a type I topoisomerase. When isolated from 32P-labeled Novikoff ascites cells or incubated in vitro with protein kinase, phosphoserine was found to be its major phosphorylated amino acid. The enzymatic activity of topoisomerase I was altered by changes in phosphorylation. Its activity was increased by protein kinase and it was decreased by alkaline phosphatase.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(83)91384-0