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

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

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

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

ASJC Scopus subject areas

  • Genetics

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