Aprotinin is a monomeric globular polypeptide derived from bovine lung tissue. It consists of a chain of 58 amino acids that fold into a stable, compact tertiary structure of the 'small SS-rich" type, containing 3 disulfides, a twisted β-hairpin and a C-terminal α-helix.
Aprotinin inhibits several serine proteases, specifically trypsin, chymotrypsin, plasmin and kallikrein. Its action on kallikrein leads to the inhibition of the formation of factor XIIa. Binding is reversible with most aprotinin-protease complexes dissociating at pH >10 or < 3. Aprotinin is freely soluble in water (>10 mg/ml) as well as low ionic strength aqueous buffers.
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