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  • Title: Thermolabile duplex-specific nuclease.
    Author: Anisimova VE, Barsova EV, Bogdanova EA, Lukyanov SA, Shcheglov AS.
    Journal: Biotechnol Lett; 2009 Feb; 31(2):251-7. PubMed ID: 18810329.
    Abstract:
    Using random mutagenesis of the gene encoding duplex-specific nuclease from the king crab we found a new mutant that retained all properties of the wild-type protein, but exhibited a much lower thermal stability. This enzyme, denoted thermolabile duplex-specific nuclease (DSN-TL), exhibits high processivity and selective cleavage of dsDNA. The inactivation temperature for DSN-TL is 15-20 degrees C lower than that of the widely used DNase I and shrimp nuclease, and its catalytic activity is more than 10 times higher. Moreover, DSN-TL is resistant to proteinase K treatment. These properties make DSN-TL very useful for removing genomic DNA from RNA samples intended for quantitative RT-PCR.
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