(1) Umezawa, H. (1976) Methods Enzymol. 45 (Part B), 678-695
Structures and activities of protease inhibitors of microbial origin.
(2) Brass, L.F. & Shattil, S.J. (1988) J. Biol. Chem. 263, 5210-5216
Inhibition of Thrombin-induced platelet activation by Leupeptin.
Leupeptin is a peptide antibiotic, isolated from several Streptomyces species. It is a reversible inhibitor of serine and cysteine proteases (e. g. plasmin, trypsin, papain, cathepsin B (1), thrombin (2), calcium-dependent protease calpain (2)). The halfmaximal inhibitory concentration (ID50) depends on the protease and ranges from 0.5 to 10 μg/ml. The working concentration is 10 - 100 μM (corresponds to 5 - 50 μg/ml), but as a starting concentration 2 μM (1 μg/ml) might be sufficient.
Stability: Leupeptin ist readily water-soluble. Aqueous stock solutions are set up with a concentration of 1 mg/ml. Leupeptin is stable in solutions at +4°C for approx. one week and at -20°C up to 6 months.