Biochem/Physiol Actions | Elastase hydrolyses elastin, the specific protein of elastic fibers, and digests hemoglobin, casein and fibrin. Elastase is a single polypeptide chain of 240 amino acid residues and contains four disulfide bridges. The molecular mass is approximately 25.9 kDa. The enzyme is synthesized as an inactive zymogen, proelastase, which is converted to the active form by limited proteolysis at the N-terminal by trypsin. It is a serine protease with broad specificity. It cleaves protein at the carboxyl side of small hydrophobic amino acids such as Ile, Gly, Ala, Ser, Val, and Leu. The enzyme also hydrolyzes amides and esters such as N-Benzoyl-L-alanine methyl ester.The pH optimum is found to be 8.0-8.5. It does not require any activator, but it is inhibited by diisopropyl fluorophosphate, phenylmethanesulfonyl fluoride, α2-macroglobulin, α1-antitrypsin, sulfonyl fluorides, p-dinitrophenyl diethylphosphate and high salt concentrations. Elastase is extensively used in tissue and cell dissociation procedures. It is effective in the isolation of Type II lung cells. |
Application | Elastase from porcine pancreas has been used in a study to identify a novel bone/calcium metabolism-regulating factor in porcine pancreas. Elastase from porcine pancreas has also been used in a study to investigate the effect of a specific synthetic inhibitor of neutrophil elastase on the course of acute hemorrhagic pancreatitis in dogs. The enzyme has been used in the proteolytic cleavage of UMP synthase (Uridine-5′-monophosphate synthase). It has also been used along with collagenase to disperse tissue into single cells from the thoracic media, abdominal aortic media and intima of rabbit. |
