Haemostatic property of new Cystein protease(s) from Sesbania grandiflora: It's action on fibrinogens

This study aims to explore possible involvement of Sesbania grandiflora leaves extract on haemostatic pathway. The crude dialyzed fraction (SgCDF) hydrolyses casein and exhibiting a protease activity (19.7 ± 1.5 U/Hr) at 100 μg/ml. Zymography (casein) studies further reveal the presence of two high molecular weight protease(s). Presence of possible protease(s) was confirmed by inhibition of Proteolytic activity by mercury chloride (HgCl2) suggesting the presence of Cysteine protease. The stability of protease activity against various parameters viz., temperature, pH, salt (NaCl) has been evaluated. These protease(s) exhibiting a promising Fibrinogenolytic activity by hydrolyzing Aα and Bβ subunit of fibrinogen at 25 μg and 50 μg concentration, whereas SgCDF fails to degrade the γ-subunit at the same concentration. The protease shows a promising recalcification time up to 80 ± 2% against Trypsin. These findings suggest the possible role of proteolytic fraction of Sesbania grandiflora in haemostatic and wound healing process.