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Partial purification and characterization of the alkaline protease of sea nettle chrysaora quinquecirrha nematocyst venom



Partial purification and characterization of the alkaline protease of sea nettle chrysaora quinquecirrha nematocyst venom



Comparative Biochemistry & Physiology C Comparative Pharmacology 74(2): 361-364



Sea nettle alkaline protease (SNP) was purified 13-fold by sequential chromatography on hexylamine Sepharose and CM-Sephadex gels. SNP had a pH and temperature optimum of 9.3.degree. and 37.degree. C, respectively, and a MW of 100,000 daltons. SNP activity was inhibited by most divalent ions, EGTA [ethylene glycol bis (.beta. aminoethyl ether) tetraacetate], EDTA and o-phenanthroline. Ca2+ reversed the inhibition of the chelators. These factors suggest that the enzyme is a metallopeptidase.

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Accession: 006066154

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DOI: 10.1016/0742-8413(83)90115-9



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