Partial purification and characterization of a DNA helicase from chloroplasts ofGlycine max
โ Scribed by Gordon C. Cannon; Sabine Heinhorst
- Publisher
- Springer
- Year
- 1990
- Tongue
- English
- Weight
- 800 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0167-4412
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โฆ Synopsis
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 Mg 2 * or Mn 2 +. Strand displacement activity does not require a free unannealed single-strand or replication fork-like structure.
๐ SIMILAR VOLUMES
Soluble DNA polymerase has been extracted from pea seedlings and partially purified by chromatography on columns of DEAE-cellulose or DEAE-Sephadex. The enzyme elutes from DEAEcellulose as a single peak, but is fractionated into three peaks, SI, SIa and SII by DEAE-Sephadex chromatography. SIa and S