Used in biochemical research to inhibit proteases during protein extraction and purification protects proteins in cell lysates radioimmunoassays and gel electrophoresis historically applied in cardiac surgery to reduce bleeding though now limited.

Primarily preserves protein integrity by blocking proteolytic degradation in lab protocols reduces fibrinolysis and inflammation by inhibiting key enzymes aiding sample stability and experimental accuracy.

Aprotinin from bovine lung is a small polypeptide (58 amino acids 6.5 kDa) extracted from bovine lung tissue featuring a compact structure stabilized by three disulfide bonds. It acts as a competitive reversible inhibitor of serine proteases like trypsin chymotrypsin plasmin and kallikrein.