Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes and blocks the active sites of serine protease enzymes. Binding is reversible with most aprotinin-protease complexes dissociating at pH >10 or < 3 (optimum pH 5-7); effective concentration is equimolar with protease. Used as a proteolytic inhibitor in radioimmunoassays of polypeptide hormones.Aprotinin is largely used as an inhibitor of trypsin.

Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes and blocks the active sites of serine protease enzymes. Binding is reversible with most aprotinin-protease complexes dissociating at pH >10 or < 3 (optimum pH 5-7); effective concentration is equimolar with protease. Used as a proteolytic inhibitor in radioimmunoassays of polypeptide hormones.
Aprotinin is largely used as an inhibitor of trypsin.