[Isolation and properties of serine proteinase PC from the Kamchatka crab, Paralithodes camtschatica--a proteolytic enzyme with broad specificity].

A homogeneous serine proteinase PC has been isolated from the Camchatka crab (Paralithodes camtschatica) hepatopancreas using affinity chromatography on arginine-Sepharose, protamine tryptic peptide-agarose and ion-exchange chromatography on Mono-Q, with a 68% yield. The enzyme is completely inhibited by diisopropylfluorophosphate, a typical inhibitor for serine proteinases. The molecular mass of the proteinase is 29 kDa, pI is 3.0. The proteinase splits Glp-Phe-Ala-pNA optimally at pH 7.5 and 47-55 degrees C; Km is 0.83 mM, kcat is 67 s-1. The enzyme is stable at pH 4-9. Proteinase PC possesses a broad substrate specificity and splits the peptide bonds formed by the carboxyl group of hydrophobic amino acids, arginine and lysine, in peptides and proteins. The enzyme hydrolyzes fibrin and collagen. Its N-terminal sequence, IVGGQEATP, reveals a 90% homology with analogous sequences of collagenolytic proteinases from other crab species.