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   <subfield code="a">DNA Polymerase βs from Liver and Testes of Cherry Salmon, Oncorhynchus masou: Purification and Characterization of DNA Polymerase βs with Acidic Isoelectric Points</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Toyofumi Yamaguchi, Shigeko Nishimura, Keiko Takahashi, Michiyasu Yoshikuni, Junya Masaki, Toshiaki Hirai, Mineo Saneyoshi]</subfield>
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   <subfield code="a">DNA polymerase βs from cherry salmon, Oncorhynchus masou, liver and testes were purified to near homogeneity, and no substantial differences between the enzymes were observed. The molecular weight of both enzymes, determined by SDS-polyacrylamide gel electrophoresis, was 39,000. The amino acid sequences of the N-terminus of the liver and testes enzymes were determined and compared with that of the rat enzyme. Of the N-terminal 30 amino acid residues of salmon liver DNA polymerase β,21 (70%) were identical to those of the rat enzyme sequence. However, unlike most eukaryotic DNA polymerase βs, the isoelectric points (pis) of the DNA polymerase βs from salmon liver and testes were both estimated to be 6.2, which is significantly different from the alkaline isoelectric points (pI=8.5-9.5) established for other highly purified vertebrate DNA polymerase βs.The cherry salmon DNA polymerase βs were still active at below 10°C, compared with the rat enzyme.</subfield>
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