LINGCOD MUSCLE NUCLEASE

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Abstract
A nuclease from muscle of lingcod (Ophiodon elongatus) has been purified by chromatography on diethylaminoethyl cellulose in the free-base form by stepwise elution with increasing concentrations of tris(hydroxymethyl)aminomethane. HCl, pH 7.0. The nuclease has been shown to hydrolyze ribonucleic acid, adenosine 3′-benzyl phosphate, thymidine 3′-p-nitrophenyl phosphate, and thymidine 5′-p-nitrophenyl phosphate. The latter compound was hydrolyzed at a very low rate. It did not hydrolyze adenosine 2′- or 5′- benzyl phosphate or certain nucleoside cyclic phosphates. The enzyme was inhibited by monoiodoacetate but not by heparin.

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