Acid proteinase activity of squid mantle muscle: some properties and subcellular distribution

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Abstract 1. 1. Acid proteinase activity of the crude extract of squid, Ommastrephes sloani pacificus, mantle muscle was measured using hemoglobin as substrate. 2. 2. The activity wax maximum at pH 2.9 and 35°C. 3. 3. Subcellular fractionation revealed that the activity was localized in lysosomes. 4. 4. The activity was inhibited strongly by pepstatin, and by iodoacetic acid and leupeptin to a small extent. The results indicated the presence of a cathepsin D-like proteinase and a thiol-proteinase, with the former retaining the major part.

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