Abstract
DNA polymerase found in an extract from eggs of the teleost fish Misgurnus fossilis (loach) has been identified as an enzyme of the γ type. The enzyme was purified 4000- to 5000-fold from the extract by liquid chromatography. The DNA polymerase activity was sensitive to the inhibiting action of aphidicolin but resistant to N2-(p-n-butylphenyl)-2´- deoxyguanosine 5´-triphosphate (BuPdGTP). The enzyme activity correlates with the presence of a polypeptide with molecular mass of 120-130 kD that interacts specifically with polyclonal antibodies against calf thymus DNA polymerase γ as revealed by Western blotting and is presumably the catalytic subunit of the enzyme. The loach DNA polymerase possesses the 3´→5´-exonuclease activity specific to single-stranded DNA and catalyzes distributive elongation of primers in primer–template complexes.
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Sharova, N.P., Dimitrova, D.D., Abramova, E.B. et al. Identification of DNA Polymerase γ in Eggs of a Teleost Fish (Loach). Biochemistry (Moscow) 66, 225–231 (2001). https://doi.org/10.1023/A:1002855917914
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DOI: https://doi.org/10.1023/A:1002855917914