METAL CONTENT AND CONFORMATION OF THE METALLOPROTEASE FROM THE MARINESPONGE SPHECIOSPONGIA-VESPARIA

We have recently purified a protease from the marine sponge Spheciospo ngia vesparia. It consists of a single nonglycosylated polypeptide cha in with a molecular weight of 29 600 and has one free thiol group. Met al analysis revealed the presence of zinc at 2.02 +/- 0.05 g-atoms per mole of protein, as measured by atomic absorption spectroscopy. The c ircular dichroism spectrum in the far UV region (183-259 nm) indicates that the sponge protease contains appreciable amounts of beta sheet. This enzyme resembles very much an aminopeptidase from Aeromonas prote olytica concerning activity and some physicochemical characteristics.