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Purification and Characterization of proteinase from Ruditapes philippinarum infected with Perkinsus sp.

In this study, we characterized a proteinase from marine bivalve Ruditapes philippinarum (Manila clam) infected with the protozoan parasite Perkinsus sp. When infected with Perkinsus sp., Manila clam produced a proteinase, which was not appeared in non-infected manila clam and Perkinsus hypnospore. A clear baiid of 45 kDa was detected on 0.2% gelatin containing gel SDS-PAGE. The proteinase was inhibited by phenylmethyl sulfonyl fluoride (PMSF) known as a serine proteinase inhibitor. Using Mucin-Sepharose CL-6B affinity chromatography, proteinases were eluted by Tris-HCl buffer (pH 7.4) containing 20 mM EDTA. Like lectins, N-acetyl-D-galactosamine also could elute proteinases. Based on these results, isolated Ruditapes philippinarum proteinase belonged to the class of serine protease and may have lectin activities or may be associated with lectin