Isolation of the catalytic core of DNA polymerase alpha from rabbit bone marrow

Lee Pletts Goscin, John J. Byrnes

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Modification of the purification procedures for rabbit bone marrow DNA polymerase [Byrnes, J.J., & Black, V.L. (1978) Biochemistry 17, 4226-4231] has increased the yield and stability of the enzyme thus allowing further purification. In particular, the higher molecular weight form, alpha1, has been more abundant. Additional purification has been obtained upon phospho-cellulose and chromatofocusing column chromatography. SDS slab gel electro-phoretic analyses of the eluates demonstrate a 135,000 molecular weight polypeptide in nearly pure form which correlates with DNA polymerase activity. Approximately 200,000 nmol of thymidine monophosphate is incorporated into DNA (mg of protein)-1h-1 at 37°C. Similar to DNA polymerase alpha from other sources this enzyme is an acidic protein, is very sensitive to aphid-icolin, and has no detectable 3′ to 5′ nuculease activity.

Original languageEnglish (US)
Pages (from-to)6023-6035
Number of pages13
JournalNucleic acids research
Issue number19
StatePublished - Oct 11 1982

ASJC Scopus subject areas

  • Genetics


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