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Nucleic Acids Research, 1975, Vol. 2, No. 11 2077-2090
© 1975

Articles

Partial purification and characterization of two cytoplasmic DNA polymerases from ungerminated wheat

M. Castroviejo, L. Tarragó-Litvak and S. Litvak

Laboratoire de Biochimie, Université de Bordeaux II, 351 Cours de la Libération 33405 Talence, France

Received September 5, 1975. Two DNA polymerases have been purified from the 105,000 x g supernatant of ungerminated wheat. The purification stages included: highspeed centrifugation, salt fractionation, DEAE-cellulose chromatography, Sephadex G-150 filtration and phosphocellulose chromatography.

Several properties of the two enzymes (called A and B according to the order of elution from the phosphocellulose column) have been studied. Enzyme A has a sedimentation coefficient of about 7 S, utilizes activated DNA and synthetic polydeoxynucleotides as well as poly rA-dT12, while B has a sedimentation coefficient of about 6.2 and uses only activated DNA and synthetic polydeoxynucleotides as templates.

Other parameters like KCl effect, MnCl2 effect, optimum pH, etc. allow us to distinguish clearly between both DNA polymerases.


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