Title: Elastase
Literature References: Serine proteases produced by many differnt cell types, named for its ability to break down the connective tissue protein elastin. Active site is a catalytic triad of residues Ser-195, His-57, and Asp-102. Hydrolyzes proteins at N-terminal peptide bonds of small aliphatic residues. First isolated from pancreatic extracts: J. Balo, I. Banga, Biochem. J. 46, 384 (1950). Amino acid sequence comparison of mammalian elastases: T. Tani et al., J. Biol. Chem. 263, 1231 (1988). Review and comparison of porcine pancreatic and human neutrophil elastase: W. Bode et al., Biochemistry 28, 1951-1963 (1989). Review of role in atherosclerosis: L. Robert et al., Atherosclerosis 140, 281-295 (1998); of role in pulmonary hypertension: M. Rabinovitch, Chest 114, Suppl., 213S-224S (1998).
Derivative Type: Pancreatic elastase
Trademarks: Elaszym (Eisai)
Literature References: Stored as an inactive zymogen in the pancreas; secreted into intestines where it is activated by trypsin and participates in digestion. Mol wt about 25,000. Porcine form is a single polypeptide chain of 240 amino acid residues and four disulfide bridges. Purification and characterization: U. J. Lewis et al., J. Biol. Chem. 222, 705 (1956); M. A. Naughton, F. Sanger, Biochem. J. 78, 156 (1961). Primary structure: D. M. Shotton, B. S. Hartley, Nature 225, 802 (1970); eidem, Biochem. J. 131, 643 (1973). Crystal structure: H. C. Watson et al., Nature 225, 806 (1970); D. M. Shotton, H. C. Watson, ibid. 811; E. Meyer et al., Acta Crystallogr. B44, 26 (1988). Review of diagnostic uses: R. Dominici, C. Franzini, Clin. Chem. Lab. Med. 40, 325-332 (2002).
Properties: White, lyophilized powder of slightly yellowish shade. pI 9.5 ±0.5. Maximum protease activity pH 8.1-8.8.
Derivative Type: Neutrophil elastase
Additional Names: Leukocyte elastase; polymorphonuclear elastase; granulocyte elastase
Literature References: Degrades extracellular matrix proteins including elastin, collagen (types I-IV), fibronectin, laminin, and proteoglycans. Necessary for migration of neutrophils through connective tissue. Defends against infectious bacteria by degrading bacterial structural proteins. Human form is a glycoprotein single peptide chain of 218 amino acid residues and four disulfide bridges. Mol wt about 33,000. Identification of elastolytic activity in polymorphonuclear leukocytes: A. Janoff, J. Scherer, J. Exp. Med. 128, 1137 (1968). Isoln and characterization: A. Janoff, Lab. Invest. 29, 458 (1973); K. Ohlsson, I. Olsson, Eur. J. Biochem. 42, 519 (1974); R. J. Baugh, J. Travis, Biochemistry 15, 836 (1976). Primary structure: S. Sinha et al., Proc. Natl. Acad. Sci. USA 84, 2228 (1987). Crystal structure: H. R. Williams et al., J. Biol. Chem. 262, 17178 (1987). Review of role in emphysema: A. Janoff, Am. Rev. Respir. Dis. 132, 417-433 (1985); of role in acute lung injury: K. Kawabata et al., Eur. J. Pharmacol. 451, 1-10 (2002).
Properties: Maximum protease activity pH 7.5-9. pI 10-11.
Elastin Elcometrine Eledoisin Elenolide Eletriptan

Space-filling model of elastase.
Crystals of porcine elastase.

In molecular biology, elastase is an enzyme from the class of proteases (peptidases) that break down proteins.[1]