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Characterization of the mitochondrial DNA polymerase from Saccharomyces cerevisiae.
Author(s) -
Surajit Sen,
Somnath Mukhopadhyay,
Jon Wetzel,
Tanmay Biswas
Publication year - 1994
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1994_4777
Subject(s) - dna polymerase , polymerase , microbiology and biotechnology , dna polymerase ii , dna polymerase i , dna clamp , primer (cosmetics) , mitochondrial dna , biology , biochemistry , primase , chemistry , dna , polymerase chain reaction , reverse transcriptase , gene , organic chemistry
The mitochondrial DNA (mtDNA) polymerase was isolated from a protease-deficient yeast strain (PY2), and purified about 3000 fold by a column chromatography on phosphocellulose, heparin-agarose, and single-stranded DNA cellulose. The purified polymerase was characterized with respect to optimal nucleotide concentrations, template-primer specificity and sensitivity to some inhibitors. These results were compared with the nuclear DNA polymerase I activity. Both polymerases showed similar requirement of deoxynucleotide concentrations (Km 5' exonuclease activity.

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