Distinction between mouse DNA polymerases α and β by tryptic peptide mapping

Stephen Planck, K. Tanabe, S. H. Wilson

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Results presented here and in a previous paper (Tanabe et al. (1979) Biochemistry 18, 3401-3406) indicate that mouse β-polymerase is a single polypeptide with an apparent molecular weight of 40,000. This polypeptide has now been analyzed by tryptic peptide mapping. comparison of the results with identical analysis of mouse α-polymerase reveals that the tryptic peptides derived from the two enzymes are different. These results indicate that β-polymerase is neither a subunit of α-polymerase nor a proteolytic degradation product of α-polymerase.

Original languageEnglish (US)
Pages (from-to)2771-2782
Number of pages12
JournalNucleic Acids Research
Volume8
Issue number12
DOIs
StatePublished - Jun 25 1980
Externally publishedYes

Fingerprint

Peptide Mapping
Polypeptides
DNA-Directed DNA Polymerase
Peptides
Mouse
DNA
Biochemistry
Enzymes
Molecular weight
Degradation
Molecular Weight

ASJC Scopus subject areas

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

Cite this

Distinction between mouse DNA polymerases α and β by tryptic peptide mapping. / Planck, Stephen; Tanabe, K.; Wilson, S. H.

In: Nucleic Acids Research, Vol. 8, No. 12, 25.06.1980, p. 2771-2782.

Research output: Contribution to journalArticle

Planck, Stephen ; Tanabe, K. ; Wilson, S. H. / Distinction between mouse DNA polymerases α and β by tryptic peptide mapping. In: Nucleic Acids Research. 1980 ; Vol. 8, No. 12. pp. 2771-2782.
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