Abstract
A DNA helicase activity was detected in extracts of purified chloroplasts from the SB-1 cell line of Glycine max and partially purified by column chromatography on DEAE cellulose, phosphocellulose, and single-stranded DNA cellulose. The chloroplast helicase has a DNA-dependent ATPase activity, and its strand displacement activity is strictly dependent upon the presence of a nucleoside triphosphate and Mg2+ or Mn2+. Strand displacement activity does not require a free unannealed single-strand or replication fork-like structure.
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Cannon, G.C., Heinhorst, S. Partial purification and characterization of a DNA helicase from chloroplasts of Glycine max . Plant Mol Biol 15, 457–464 (1990). https://doi.org/10.1007/BF00019162
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DOI: https://doi.org/10.1007/BF00019162