Isolation and characterization of rat pancreatic elastase.
Proelastase has been purified to homogeneity from rat pancreatic tissue by a combination of CM-Sephadex and immobilized protease inhibitor affinity resins. Trypsin activation yields an elastolytic enzyme that possesses a specificity toward small hydrophobic residues in synthetic amide substrates, similar to those of porcine elastase 1 and canine elastase. However, the rat enzyme also rapidly hydrolyzes a substrate containing tyrosine in the P1 position. N-Terminal sequence analysis reveals that rat proelastase has an identical activation peptide with that of porcine proelastase 1 and has two conservative amino acid sequence differences from the activation peptide of canine proelastase. The sequence data established that rat proelastase corresponds to the elastase 1 mRNA clone isolated by MacDonald et al. [MacDonald, R. J., Swift, G. H., Quinto, C., Swain, W., Pictet, R. L., Nikovits, W., & Rutter, W. J. (1982) Biochemistry 21, 1453]. The sequence and substrate data obtained for rat and canine elastases suggest that there is a family of pancreatic elastases with properties similar to those of the classically described porcine elastase 1.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004285:Dogs; D004792:Enzyme Precursors / Q000302:isolation & purification; D006801:Humans; D007700:Kinetics; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D013045:Species Specificity; D013379:Substrate Specificity; D013552:Swine
D000596:Amino Acids; D004792:Enzyme Precursors; D010196:Pancreatic Elastase