Description
Analysis Note Leupeptin gives multiple peaks on HPLC due to equilibria among three forms in solution. Purity determined using three main peaks. Majority of contaminating peptide is racemized leupeptin.
Biochem/physiol Actions Inhibitor of serine and cysteine proteases. Inhibits plasmin, trypsin, papain and cathepsin B. No inhibition found with pepsin, cathepsins A and D, thrombin, or α-chymotrypsin. Effective concentration 10-100 μM.
Properties
biological source microbial
assay ≥90% （HPLC）
EQP level Premium
solubility H2O: 10 mM （Solutions are stable for a week at 4 °C. Stock solutions are stable up to 6 months at −20 °C.）
storage temp. −20°C
Safety
Personal Protective Equipment Eyeshields, Gloves, type N95 （US）, type P1 （EN143） respirator filter
Safety Statements 22-24/25
WGK Germany 3
References
reference Aoyagi, T., Inhibitor of trypsin, plasmin, papain and cathepsin B. J. Antibiot. 22, 283, （1969）
Saino, T., et al. Chem. Pharm. Bull. 30, 2319, （1982）
Deutscher, M.P., Maintaining protein stability. Meth. Enzymol. 182, 83-89, （1990）
Jazwinski, S.M., Preparation of extracts from yeast. Meth. Enzymol. 182, 154-174, （1990）
, Beynon, R.J. and Bond, ed. Proteolytic Enzymes: A Practical Approach, （1989）, 244-245
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