Eukaryotic DNA polymerase alpha. Structural analysis of the enzyme from regenerating rat liver
The DNA polymerase alpha from regenerating rat liver has been purified to near homogeneity. The most highly purified fraction gave a single stained band on native polyacrylamide gel electrophoresis, and DNA polymerase alpha activity was coincident with this band. On pore gradient gel electrophoresis...
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Published in | The Journal of biological chemistry Vol. 255; no. 5; pp. 2114 - 2122 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Biochemistry and Molecular Biology
10.03.1980
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Subjects | |
Online Access | Get full text |
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Summary: | The DNA polymerase alpha from regenerating rat liver has been purified to near homogeneity. The most highly purified fraction
gave a single stained band on native polyacrylamide gel electrophoresis, and DNA polymerase alpha activity was coincident
with this band. On pore gradient gel electrophoresis, a molecular radius of 72 A was obtained for the enzyme. On denaturing
sodium dodecyl sulfate-polyacrylamide gel, five polypeptides were reproducibly resolved, corresponding to molecular weights
of 156,000, 64,000, 61,000, 58,000, and 54,000. The catalytic subunit correlated with the 156,000-dalton polypeptide. In the
native state, the separated 54,000- to 64,000-dalton polypeptides interacted among themselves to constitute a hetero oligomer
of apparent high molecular weight without DNA polymerase activity. Electron microscopy studies of the enzyme confirmed the
biochemical results. The specific activity of the isolated catalytic subunit was in all cases lower than when it was associated
with the 54,000- to 64,000-dalton structure. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)86001-5 |