Abstract
1. 1. Proteases from the digestive gland of the mussel Perna perna were subjected to an isolation procedure similar to that used for mammalian thiol cathepsins. 2. 2. A protease was purified by ammonium sulphate fractionation, molecular exclusion chromatography and ion exchange chromatography on CM-Sephadex. 3. 3. The enzyme was activated by thiol-reducing agents and metal chelators, inhibited by iodoacetamide, N-ethylmaleimide, divalent mercury ions and TPCK, at high concentration, and is therefore apparently a thiol protease. It is not affected by leupeptin or pepstatin. 4. 4. The enzyme has a MW of 21,000 and digests azocasein, with an acidic pH optimum, but is not active against either l-arginine β-naphthylamide or l-arginyl- l-arginine β-naphthylamide.
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