作者: Misako Sasakuma , Arland E. Oleson
DOI: 10.1016/0031-9422(79)83074-5
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摘要: Abstract 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. inhibited by several adenine nucleotides, and it binds weakly to NADP-agarose ATP-agarose.