Human Leukocyte Elastase-Like Proteinase Purified by Affinity Chromatography with Suc-L-Tyr-D-Leu-D-Val-pNA, and Its Identification with Human Spleen Fibrinolytic Proteinase

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Abstract
Elastase-like proteinase (ELP) extracted with 2 M NaClO4 from human leukocytes was purified by a new affinity chromatography technique with Suc-L-Tyr-D-Leu-D-Val-pNA, following delipidation, salting out and Sephadex gel chromatography. The purified preparation contained practically no chymotrypsin-like proteinase activity, and it was homogeneous on SDS polyacrylamide gel electrophoresis. The enzyme so purified readily degraded fibrin, fibrinogen, elastin and -Val type synthetic peptide substrates, such as Suc-L-Ala-L-Tyr-L-Leu-L-Val-pNA and Suc-L-Tyr-L-Leu-L-Val-pNA. A special increase in ELP activity by adding chaotropic ions was observed. The enzymatic properties of the ELP were very similar to those of spleen fibrinolytic proteinase (SFP). ELP and SFP were identified immunologically using mice antisera against purified ELP.