Purification and antithrombotic activity of wulfase, a fibrinolytic enzyme from the fruit bodies of the edible and medicinal mushroom Sparassis crispa Wulf. ex. Fr.

Abstract

A fibrinolytic protease, wulfase, exhibiting antithrombotic potency was purified from the fruit bodies of Sparassis crispa Wulf. ex. Fr. Wulfase showed a single band of approximately 90 kDa by SDS-PAGE and fibrin zymography. The fibrinolytic activity of wulfase determined by fibrin plate assay revealed that it could directly degrade fibrin clot. The enzyme could inhibit activities of factor Xa and thrombin. Turbidity and electron-microscopy analysis using fluorescent conjugate demonstrated that wulfase also inhibited fibrin polymer formation. The anticoagulant effect of the enzyme was further confirmed in human plasma. These results suggest that wulfase may be useful for reducing or preventing thrombotic challenge.