I. Turkey ovomucoid and chicken ovoinhibitor which have been found to be inhibitors of bovine trypsin and a-chymotrypsin can inhibit the esterolytic, proteolytic and elastolytic activities of porcine elastase. The formation of the complex between the elastase and each inhibitor could be demonstrated by means of electrophoresis a t p H 6.9. The complexes are formed in molar ratios of one to one. They are stable and no temporary inhibition could be observed.2. The complexes of porcine elastase with turkey ovomucoid and chicken ovoinhibitor inhibit bovine trypsin a t the same molar ratio as free inhibitors. The complexes of trypsin with these inhibitors inhibit elastase as do the free inhibitors. The complex of porcine elastase with turkey ovomucoid does not inhibit bovine chymotrypsin and the complex of chymotrypsin with this inhibitor does not inhibit elastase. The complex of porcine elastase with chicken ovoinhibitor inhibits bovine chymotrypsin but not the alkaline proteinase from Aspergillus sojae. The complex of this inhibitor with bovine chymotrypsin inhibits the porcine elastase while the complex iwith alkaline proteinase does not.It was concluded, therefore, that turkey ovomucoid has two independent binding sites, one for trypsin and the other for chymotrypsin or elastase and that chicken ovoinhibitor has three independent binding sites, one for trypsin, another for chymotrypsin and a third one for either elastase or alkaline proteinase.3. The complexes between porcine elastase and turkey ovomucoid or chicken ovoinhibitor are not adsorbed on elastin whereas elastase is.
4.Kunitz soybean and pancreatic trypsin inhibitors, Birk-Bowman soybean trypsin and chymotrypsin inhibitor, groundnut and h a bean trypsin and chymotrypsin inhibitors do not inhibit the esterolytic, proteolytic and elastolytic activities of porcine elastase, even in weight ratios in excess of 10 : 1.Although the tertiary structure and the catalytic site of porcine elastase are similar to those of bovine trypsin and chymotrypsin, its binding site and substrate specificity are quite different [I, 21. Elastase is not inhibited by most of the natural trypsin and chymotrypsin inhibitors [3]. Several reports described inhibition of porcine elastase by trypsin inhibitors from plants or animals 14-81 but in most cases only the non-specific proteolytic activity was inhibited while the elastolytic activity was almost unaffected An introduction of a highly specific esterase substrate for porcine elastase, N-acetyl-L-alanyl-Lalanyl-L-alanine methyl ester [I21 enhanced our studies on specific inhibition of porcine elastase by natural inhibitors.The present study describes the inhibition of porcine elastase by turkey ovomucoid and chicken ovoinhibitor and partial characterization of their complexes with this enzyme.