RIBONUCLEASE ACTIVITY OF FISH MUSCLE EXTRACTS

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Abstract
A ribonuclease was partially purified from muscle of lingcod (Ophiodon elongatus). The preparation degraded yeast and lingcod ribonucleic acid. Four 3[image] -mononucleotides were identified as digestion products. The enzyme was readily destroyed by heat and acid (10 minutes at 58[degree]C, pH 2.5), and was inhibited strongly by Zn++, Cu++, monoiodoacetate, formaldehyde, and NaF. Its pH optimum was 6.5. Ribonuclease activity was also demonstrated in muscle extracts from spring salmon, lemon, sole, dogfish, sculpln, herring, and swordfish. The muscle extracts of all fish examined possessed phosphodiesterase activity. The ribonuclease in lingcod extract could be separated from two phosphodiesterases also present by zone electrophoresis.