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https://doi.org/10.1016/0031-9422(79)83074-5
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Cite Journal: Phytochemistry |  Publication Date: Jan 1, 1979 |
 Citations: 7 |
Affiliation: North Dakota State University
A sugar-unspecific nuclease has been purified 260-fold from barley malt diastase. The enzyme, a glycoprotein of 37 000 MW, is highly active on single-stranded polynucleotides at pH 5–6. The nuclease is inhibited by several adenine nucleotides, and it binds weakly to NADP-agarose and ATP-agarose.
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