The debriding activity of the protease complex produced from the hepatopancreas of the king crab Paralithodes camtschatica was evaluated in vivo. The results clearly showed that the crab preparation had a high debriding ability. Individual proteases were isolated chromatographically from the crab complex to compare their debriding activities. All the purified proteases were active in vivo. The most active component of the complex was the isozyme C of crab collagenolytic protease, a member of the chymotrypsin-like protease class.

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Immunohistochemical study of tissues from purulent wounds in rats after treatment with the collagenase isolated from the King crab Paralithodes camtschatica was undertaken. The enzymotherapy resulted in a rapid and efficient removal of necrotic debris. It was accompanied by fibrin elimination from the wound bed and subsequent formation of new capillaries. Cellular fibronectin with ED-A sequence was identified in the newly formed granulation tissue, which points to its active synthesis in situ. Polyclonal antibodies against two isozymes of the crab collagenolytic protease were obtained. By their use it was shown that, after application of the collagenase, both isozymes accumulated in fibrin deposits at the wound bed but did not penetrate adherent granulation tissue.