Abstract
A sample of highly purified calf thymus alpha-polymerase contained an abundant 118,000 Mr polypeptide as well as five lower molecular weight polypeptides in the range of 54,000- to 64,000-Mr. This 118,000-Mr polypeptide was capable of DNA polymerase activity, as revealed by in situ assay after SDS-polyacrylamide gel electrophoresis. Tryptic peptide mapping indicated that the 118,000-Mr polypeptide shared extensive primary structure homology with 57,000-, 58,000- and 64,000-Mr polypeptides and some limited homology with 54,000- and 56,000-Mr polypeptides. This is the first evidence that lower and higher Mr polypeptides of purified calf thymus alpha-polymerase share sequence homology; these results are interpreted in the context of a model that predicts the existence of a common precursor with molecular weight greater than 140,000.
MeSH Terms
Animals
Cattle
DNA Polymerase II/isolation & purification
DNA-Directed DNA Polymerase/isolation & purification
Electrophoresis, Polyacrylamide Gel
Macromolecular Substances
Molecular Weight
Peptide Fragments/analysis
Thymus Gland/enzymology
Trypsin
Chemicals
Macromolecular Substances
Peptide Fragments
DNA Polymerase II
DNA-Directed DNA Polymerase
Trypsin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Albert W
Grummt F
Hübscher U
Wilson S H
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