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  • Title: BAL 31 nuclease as a probe in concentrated salt for the B-Z DNA junction.
    Author: Kilpatrick MW, Wei CF, Gray HB, Wells RD.
    Journal: Nucleic Acids Res; 1983 Jun 11; 11(11):3811-22. PubMed ID: 6304643.
    Abstract:
    The BAL 31 nuclease, an extracellular nuclease from A. espejiana, specifically recognizes and cleaves the salt induced conformational junction between B and Z-DNA. Short segments of (dC-dG) left-handed Z-helix, comprising approximately 1% of the total DNA, are specifically detected within two different recombinant plasmids. The BAL 31 enzyme is highly resistant to inactivation by the presence of high concentrations of a variety of electrolytes that stabilize left-handed helices, is active at physiological pH, and can be used to probe both linear and circular DNAs. Additionally, the nuclease cleaves left-handed (dC-dG)n only very poorly, if at all. Thus, the BAL 31 nuclease can be utilized as a probe for helical junctions and consequently for segments of left-handed DNA that might exist within predominantly right-handed naturally occurring genomes.
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