Pancreatic Trypsin Inhibitor Trypsin-Kallikrein Inhibitor White to off-white crystalline solid. HYGROSCOPIC. A competitive and reversible inhibitor of esterases and proteases. Forms a tight complex with and blocks the active site of the enzymes. Inhibits a number of different proteases, including chymotrypsin, coagulation factors involved in the prephase of blood clotting, kallikrein (Kd = 1 x 10-7 M), plasmin (Kd = 2.3 x 10-10 M) , tissue and leukocytic proteinases, and trypsin (Kd = 5 x 10-14 M). Does not inhibit Factor Xa and thrombin. It is relatively acid- and heat-stable. Useful as a serine protease inhibitor during purification of proteins and in studies of zymogen activation systems. Activity: ≥5500 KIU/mg dry weight. One Kallikrein Inhibitory Unit (K.I.U.) is defined as the quantity of protease inhibitor that will inhibit two kallikrein units by 50% under optimal conditions. Note: 1 KIU = 0.025 antiplasmin units (APU) or 0.0031 trypsin inhibitor units. Purity: ≥95% by gel filtration. Contaminants: endotoxin: ≤10 EU/mg. Effectively inhibits target proteases at equimolar concentration. pH optimum 5 - 7, pI 10.5. RTECS YN5080000, CAS 9087-70-1. Note: 1 K.I.U. = 0.025 antiplasmin units (APU) or 0.0031 trypsin inhibitor units. Merck Index: 14, 757 Ref.: Roberts, R.F., et al. 1998. Ann. Thorac. Surg. 66, 225. Azougagh Oualane, F., et al. 1992. Thromb. Res. 68, 185. Anderson, L.O., et al. 1986. Proc. Natl. Acad. Sci. USA 83, 2979. Kruithof, W.L., et al. 1986. Biochem. J. 226, 631. McKeehan, W.L., et al. 1986. J. Biol. Chem. 261, 5378. Fritz, H., and Wunderer, G. 1983. Arzneim. Forsch. 33, 479. Rijken, D.C., and Collen, D. 1981. J. Biol. Chem. 256, 7035. Kassell, B., et al. 1970. Methods Enzymol. 19, 845. |