Conservation of Molecular Structure of DNA Polymerase β in Vertebrates Probed by Tryptic Peptide Mapping

• Published in: Journal of biochemistry (Tokyo) 1984-01, Vol.96 (2), p.365-370
• Main Authors: TANABE, Kazushi, YAMAGUCHI, Toyofumi, SANEYOSHI, Mineo, YAMAGUCHI, Masamitsu, MATSUKAGE, Akio, TAKAHASHI, Taijo
• Format: Article
• Language: English
• Subjects: amino acid sequence; Analytical, structural and metabolic biochemistry; Animals; Antigen-Antibody Complex; Biological and medical sciences; Chick Embryo; DNA polymerase; DNA Polymerase I - metabolism; electrophoresis; Enzymes and enzyme inhibitors; Female; Fundamental and applied biological sciences. Psychology; Immune Sera; Male; Mice; Ovary - enzymology; Peptide Fragments - analysis; peptide mapping; Plasmacytoma - enzymology; Rana catesbeiana; Salmon; Species Specificity; Testis - enzymology; Transferases; Trypsin; Vertebrata
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a134846

DNA polymerase β's from mouse myeloma, chick embryo, and cherry salmon testis were all composed of a single polypeptide of about 40K daltons as judged by a sodium dodecyl sulfate-polyacrylamide gel electrophoresis of extensively purified enzyme preparations. Although the enzyme from bullfrog ovary was not fully purified, its molecular weight was estimated to be the same as that of the chick enzyme by immunological detection after electrophoresis. All the enzymes tested cross-reacted immunologically with the antibody against chick DNA polymerase β, indicating that they have a common molecular structure, at least in part. Two-dimensional maps of radioiodinated tryptic peptides directly showed the presence of highly conserved amino acid sequences among mouse, chick, and cherry salmon enzymes. This conserved structure is thought to be essential for the enzyme activity, which is very similar among all these vertebrates.