POLY(DT)-STIMULATED ATPASE ACTIVITY ASSOCIATED WITH SIMIAN VIRUS-40 LARGE T-ANTIGEN
- 1 January 1979
- journal article
- research article
- Vol. 254 (17) , 8113-8116
Abstract
Highly purified SV40 large T [tumor] antigen exhibits ATPase activity which can be stimulated approximately 7-fold by the DNA homopolymer poly(dT). The poly(dT)-stimulated enzyme can hydrolyze various ribonucleotide and deoxyribonucleotide triphosphates, with ATP and dATP serving as the best substrates. Purified large T antigen hydrolyzes ATP to ADP and Pi, with a maximum specific activity of 13.5 .mu.mol of inorganic phosphate released/h/mg of protein. Of the various natural and synthetic polynucleotides tested, poly(dT) was by far the best activator. Long chain poly(dT) molecules are much more effective activators than are short chain length oligo(dT) molecules. Highly purified large T antigen contains no detectable protein kinase activity.This publication has 6 references indexed in Scilit:
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