Aprotinin in Solution from Bovine Lung 10mL

Aprotinin is a natural inhibitor of trypsin, chymotrypsin and plasmin. It is found in bovine lymph nodes, lung, parotid gland, spleen, liver, pancreas, seminal vesicles, thyroid gland, kidney, mucous membranes of the trachea and esophagus, ovaries, heart, posterior pituitary and cartilage. A serine protease inhibitor which is reactive against trypsin, chymotrypsin, plasmatic and glandular kininogenases, plasmin, kallkrein, urokinase, clotting factor XIIa, protein C, proteinases of the complement system, and leukocyte and tissue proteinases. It does not inhibit thrombin. Aprotinin works by blocking the active sites of enzymes. Binding is reversible with most aprotinin-protease complexes dissociating at pH > 10 or < 3. Aprotinin is a competitive serine protease inhibitor that forms stable complexes with and blocks the active sites of enzyme. This binding is reversible, and most aprotinin-protease complexes will dissociate at extreme pH levels >10 or <3. Structurally, Aprotinin is a monomeric globular protein derived from bovine lung that consists of 58 amino acids, arranged in a single polypeptide chain with three crosslinking disulfide bridges.