A PROTEASE INHIBITOR FROM MOMORDICA CHARANTIA DIFFERENTIALLY INHIBITS TRYPSIN, ELASTASE AND CATHEPSIN G (SERINE PROTEASES) HAVING REGULATORY ROLE IN INFLAMMATION

Serine proteases are known to have significant role in inflammation. Their dysregulation may result in various inflammatory diseases. They are released from activated leukocytes and mast cells. Effects of serine proteases are mediated by Proteaseactivated receptors (PARs). Studies have been carried out on serine proteases as therapeutic target for regulation of inflammation by inhibiting serine proteases. Prolonged usage of synthetic drugs shows various side effects. Thus, plants or natural compounds are being explored as an alternative with minimum side effects. The present study focuses on a serine protease inhibitor isolated from the fruit of Momordica charantia by ammonium sulphate precipitation method and further purified using gel filtration chromatography on sephacryl S-100. A 3.07 fold purification of serine protease inhibitor with a yield recovery of 12.9% was achieved. The molecular mass of the purified serine protease inhibitor was approximately 28kDa as determined by 12.5% SDS-PAGE. The purified serine protease inhibitor showed 100% trypsin, 91% cathepsin G and 55% elastase inhibition activity. The isolated inhibitor exhibits maximum inhibition activity at 25?. Thus isolated inhibitor may have potential to be developed as therapeutic against inflammation