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J. Biol. Chem., Vol. 262, Issue 33, 16105-16108, Nov, 1987

DNA polymerase-primase from embryos of Drosophila melanogaster. DNA primase subunits

S Cotterill, G Chui and IR Lehman
Department of Biochemistry, Stanford University School of Medicine, California 94305.

The primase associated with the DNA polymerase-primase of Drosophila melanogaster fails to show enzymatic turnover. However, it does show turnover when dissociated from the intact polymerase-primase. Both forms of the enzyme can catalyze the synthesis of primers that are not complementary to the DNA template. Like the intact enzyme, the isolated primase synthesizes primers of a unique chain length; however, they are twice as long as those synthesized by the polymerase-primase. The activity of the primase separated from the polymerase-primase is similar in all other respects to the intact polymerase-primase.
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