Multiple deoxyribonucleic acid polymerases from quiescent wheat embryos. Purification and characterization of three enzymes from the soluble cytoplasm and one from purified mitochondria.
Three DNA polymerases (A, B and C) have been purified from the soluble cytoplasm of ungerminated embryos. Mainly on the basis of chromatographic, template-specificity and salt-inhibition evidence, we have characterized the three enzymes. Other physico-chemical and enzymic properties are described. From purified mitochondria we have purified a DNA polymerase that behaves like DNA polymerase B on chromatographic and template-specificity criteria. Only highly purified enzyme B from the soluble cytoplasm showed an exonuclease activity able to degrade 3'- or 5'-labelled polydeoxyribonucleotides, as well as a 'proof-reading' capacity.
D002852:Chromatography, Ion Exchange; D003593:Cytoplasm / Q000201:enzymology; D004259:DNA-Directed DNA Polymerase / Q000302:isolation & purification* / Q000378:metabolism; D005092:Exonucleases / Q000378:metabolism; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology; D012639:Seeds / Q000201:enzymology*; D013698:Templates, Genetic; D014908:Triticum / Q000201:enzymology
D007527:Isoenzymes; D004259:DNA-Directed DNA Polymerase; D005092:Exonucleases