Partial purification and characterization of the alkaline protease of sea nettle (Chrysaora quinquecirrha) nematocyst venom

Abstract

1. Sea nettle alkaline protease (SNP) was purified 13-fold by sequential chromatography on hexylamine Sepharose and CM-Sephadex gels. 2. SNP had a pH and temperature optimum of 9.3 and 37°C respectively and a molecular weight of 100,000 daltons. 3. SNP activity was inhibited by most divalent ions, EGTA, EDTA and o-phenanthroline. Calcium ion reversed the inhibition of the chelators. These factors suggest that the enzyme is a metallopeptidase.