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

Stephen R. Planck | Zendy; K Tanabe | Zendy; Samuel H. Wilson | Zendy

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

Author(s) -

Stephen R. Planck,

K Tanabe,

Samuel H. Wilson

Publication year - 1980

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/8.12.2771

Subject(s) - biology , polymerase , dna polymerase , polymerase chain reaction , microbiology and biotechnology , biochemistry , protein subunit , enzyme , gene

Results presented here and in a previous paper (Tanabe et al. (1979) Biochemistry 18, 3401--3406) indicate that mouse beta-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 alpha-polymerase reveals that the tryptic peptides derived from the two enzymes are different. These results indicate that beta-polymerase is neither a subunit of alpha-polymerase nor a proteolytic degradation product of alpha-polymerase.

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