Xa, Xlla, kallikrein, plasmin, trypsin

Bik inhibits the trypsin serine proteases through binding of either of its two Kunitz domains. Depending on the serine protease and the Kunitz domain involved, dissociation constants (K ) range from 0.03 to 800 pM [6, 28]. Bik fragmentation and glycation also effect strength and specificity of inhibition. For example, trypsin, chymotrypsin, kallikrein, plasmin, elastase, and cathepsin are inhibited at a A) of 0.03-3 pM, whereas Factors IXa, Xa, XIa, and Xlla are less inhibited with a A) of 15-800 pM. Protease inhibition is observed with both Kunitz domains except for Factors IXa and Xa that... 

Antithrombin (AT) is a serine protease inhibitor that inhibits thrombin, factor Xa, IXa, XIa, Xlla, tPA, urokinase, trypsin, plasmin, and kallikrein (Lahiri et al. 1976 Travis and Salvesen, 1983 Menache, 1991 Menache et al. 1992). Human Antithrombin of molecular weight equal approximately to 58,000 Da, contains 432 amino acids, three disulfide bridges, and four carbohydrate side chains, which account for 15% of the total mass (Magnusson, 1979 Franzen et al. 1980). Human antithrombin is synthesized in the liver and present in plasma at levels of 14 to 20mg/dl (Murano et al. 1980 Rosenberg et al. 1986). One cause of decreased level of antithrombin is pathological conditions. 

Tincture of the dried seed, on agar plate at a concentration of 30 p,L/disc, was inactive on Escherichia coli, Pseudomonas aeruginosa, and Staphylococcus aureus. Extract of 10 g plant material in 100 mL ethanol was used b Anticoagulation activity. Serpin BSZx (an inhibitor of trypsin and chemotrypsin) inhibited thrombin, plasma kallikrein, factor Vlla/tissue factor, and factor Xa at heparin-independent association rates. Only factor Xa turned a significant fraction of BSZx over as substrate. Activated protein C and leukocyte elastase were slowly inhibited by BSZx, whereas factor Xlla, urokinase and tissue type plasminogen activator, plasmin and pancreas kallikrein, and elastase were not or only weakly affected. Trypsin from Fusarium was not inhibited, while interaction with subtilisin Carlsberg and Novo was rapid, but most BSZx was cleaved as a substrate L... 

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