Purification and Properties of Whale Pancreatic Ribonucleases

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Abstract
Two ribonucleases, (RNase W1 and W2), were Isolated from whale pancreas. They were purified by CM [carboxymethylj-cellulose column chromatography 60 and 91 fold, respectively. RNases W1 and W2 were different from RNase A in respect of the elution position on CM-cellulose column chromatography, optimum temperature (5[degree]C lower than RNase A), pH optima on using C-cyclic-p as substrate (pH 6.0) and specific activities. Two whale RNases have properties very similar to that of RNase A in respect of molecular weight, heat stability and isoelectric point. The whale enzymes have base specificities similar to that of RNase A and are markedly inhibited by CU++ Zn++ and Hg++.