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The Specificity of a Nuclease from Chicken Pancreas

From the ¹ From the Institute of Cellular Biology, Univesity of Connecticut, Storrs, Connecticut 06268

The specificity of a chicken pancreas nuclease free from phosphodiesterase and nucleotidase activity was studied. The enzyme did not hydrolyze 2',3'-cyclic phosphates of guanosine, cytidine, or uridine. It rapidly hydrolyzed polyadenylate and more slowly polyuridylate, producing mainly di- and trinucleotides. Little or no mononucleotides were produced. Studies on hydrolysis of ribonucleic acid and deoxyribonucleic acid suggested that the enzyme is mainly an endonuclease which forms short chain oligonucleotides (di-, tri-, and tetranucleotides) that terminate in 5'-phosphate and 3'-hydroxyl. There is little or no bond specificity. Exhaustive digests of RNA do produce some mononucleotides, but the rate of mononucleotide production is very slow. The properties of this pancreatic enzyme were compared to other nucleases.

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