Drosophila DNA polymerase delta: purification and characterization
1994
Aoyagi, N. | Matsuoka, S. | Furunobu, A. | Matsukage, A. | Sakaguchi, K.
A DNA polymerase with properties similar to mammalian polymerase delta has been isolated to near homogeneity from early embryos of Drosophila melanogaster. A combination of exclusion chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicates that this enzyme has a total molecular mass of 185 kDa and is composed of 138- and 47-kDa polypeptides. Its isoelectric point is 6.8. This polymerase activity is strongly inhibited by N-ethylmaleimide, aphidicolin, and high KCl concentration but is relatively insensitive to 2',3'-dideoxythymidine 5'-triphosphate. There was no reaction in an immunological test using monoclonal antibody against Drosophila DNA polymerase alpha. In a final purification step, this polymerase activity was accompanied by 3' leads to 5'-exonuclease activity as expected proofreading activity. This polymerase activity is remarkably stimulated by mouse proliferating cell nuclear antigen, which is structurally and imrnunologically very similar to a Drosophila counterpart. These properties clearly indicate this enzyme belongs to the category of DNA polymerase delta.
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