Elastase is prepared from porcine pancreas. It is lyophilised and water soluble. Elastase is chromatographically prepared by the method of Narayanan and Anwar. In the method, 2 times crystalline elastase is adsorbed on a column of DEAE-Sephadex A50 to separate elastase and non-specific protein components. The elastase component is further purified by chromatography on a column of CM-Cellulose using a sodium chloride gradient to elute the elastase. The latter is dialysed until chloride-free and then lyophilised. During its preparation the elastase is held below a pH of 5,5 for greater than 24 hours. Two times crystallised from the euglobin fraction of porcine pancreas by the method of Lewis et al. Does not contain trypsin or chymotrypsin.
- Inhibitors: DFP, elastinal, α-2-macroglobulin
Elastase is an enzyme from the class of proteases (peptidases) that break down proteins. It hydrolyses peptide bonds, especially those adjacent to neutral amino acids.
Elastase was used to study human emphysema by induction of emphysema in rodents. It has been used in a study to investigate the design, synthesis and evaluation of biomimetic affinity ligands for elastases. Elastase from porcine pancreas has also been used in a study to investigate the purification and partial characterisation of the pancreatic proteolytic enzymes trypsin, chymotrypsin, and elastase. It hydrolyses peptide bonds, especially those adjacent to neutral amino acids.
Elastase hydrolyses elastin, the specific protein of elastic fibers, and digests hemoglobin, casein and fibrin.