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Abstract
A protease has been purified from the latex of Euphorbia supina Rafin by two steps of chromatography. The M r was estimated by SDS-PAGE to be 80 kDa. Its activity was inhibited strongly by diisopropyl fluorophosphate, but not by EDTA, pepstatin, or cysteine protease inhibitors, indicating that the enzyme is a serine protease. The specificity of the protease is broad, but the preferential cleavage sites were C-terminal sites of hydrophobic amino acid residues. The N-terminal sequence of the first fifteen residues was determined and six of the residues match those in cucumisin [EC 3.4.21.25], a protease from the sarcocarp of melon fruit ( Cucumis melo L. var. Prince). The results indicate that the E. supina protease is a cucumisin-like serine protease.
Published Version
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