Phosphorylation of purified Novikoff hepatoma topoisomerase I |
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Authors: | E Durban J S Mills D Roll H Busch |
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Affiliation: | Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030 USA |
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Abstract: | 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. |
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