| abstract |
A serine protease inhibitor protein is disclosed which is a purified, single-polypeptide-chain protein having at least one active site possessing serine protease inhibitor activity. This serine protease inhibitor exhibits substantial homology to the native serine protease inhibitor isolated from parotid secretions and is resistant to denaturation by heat and acids and resistant to proteolytic enzymes. The serine protease inhibitor also has the ability to re-fold into an active form after complete reduction of the disulfide bonds of the inhibitor and denaturation of all non-covalent interactions that would otherwise serve to stabilize the tertiary structure of the inhibitor after removal of these conditions. Additionally, a method for isolation of the purified serine protease inhibitor is set forth. Analogs of the serine protease inhibitors in which the amino acid sequence is varied slightly are also disclosed, which analogs variously show improved properties including improved resistance to oxidative inactivation, improved ability to inhibit pancreatic elastase, improved ability to inhibit cathepsin G, and improved ability to inhibit trypsin. |