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

Lee Pletts Goscin, John Byrnes

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

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
Pages (from-to)6023-6035
Number of pages13
JournalNucleic Acids Research
Volume10
Issue number19
DOIs
StatePublished - Oct 11 1982

Fingerprint

Catalytic DNA
DNA Polymerase I
DNA-Directed DNA Polymerase
Rabbit
Purification
Bone
Isolation
Catalytic Domain
DNA
Molecular Weight
Bone Marrow
Thymidine Monophosphate
Rabbits
Enzyme Stability
Aphids
Enzymes
Molecular weight
Cellulose
Biochemistry
Protein

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Health, Toxicology and Mutagenesis
  • Toxicology
  • Genetics(clinical)
  • Genetics

Cite this

Isolation of the catalytic core of DNA polymerase alpha from rabbit bone marrow. / Goscin, Lee Pletts; Byrnes, John.

In: Nucleic Acids Research, Vol. 10, No. 19, 11.10.1982, p. 6023-6035.

Research output: Contribution to journalArticle

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