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Suc-Tyr-Leu-Val-pNA and Suc-Ala-Tyr-Leu-Val-pNA were reported as the synthetic substrates specific for spleen fibrinolytic proteinase (SFP) and also leucocyte elastase-like proteinase (ELP). The present paper deals with reversible and irreversible synthetic inhibitors of ELP which were designed, based on the amino acid sequence of the substrates, and the application of one of the inhibitors for the purification of ELP. Among the various stereoisomers of Suc-Tyr-Leu-Val-pNA and Suc-Ala-Tyr-Leu-Val-pNA examined, Suc-L-Tyr-D-Leu-D-Val-pNA was the most effective and highly specific inhibitor. Based on these properties of the inhibitor to ELP, the affinity chromatographic purification of the enzyme was performed employing the inhibitor-Sepharose. The ELP preparation partially purified by delipidation, salting out and gel chromatography was applied on the affinity column equilibrated with Tris-HCl buffer (0.1M, pH 8.0) containing 0.5M NaClO4. Adsorbed protein was eluted by the buffer containing 8M urea. It was noteworthy that the ELP preparation thus obtained showed a single band by SDS-PAGE and contained neither collagenase nor cathepsin G.Concerning with irreversible inhibitors of ELP, chloromethyl ketone derivatives of Tyr-Leu-Val- and Ala-Tyr-Leu-Val- type peptides were synthetized. Among the compounds tested, Boc-L-AIa-L-Tyr-L-Leu-L-Val-CH2Cl showed the strongest inhibitory effect on the enzyme.The reversible and irreversible inhibitors reported here inhibited the hydrolysis of specific synthetic substrates and fibrin by either ELP or SFP.

New synthetic inhibitors of leucocyte elastase-like proteinase (ELP): Application to the purification method of ELP