SUMMARY: Large amounts of a highly purified, extracellular elastolytic protease of were obtained by sequential ammonium sulphate precipitation and hydrophobic interaction chromatography with phenyl-Sepharose CL-4B. The protease had an of about 50500 (estimated by SDS-PAGE), a pI of 5·7, and a temperature optimum range of 55 to 60 °C. The pH optimum and the results of inactivation studies suggested that the enzyme was a neutral metalloprotease. The protease had about 429 amino acid residues, and the first 20 amino-terminal amino acid residues were Ala-Gln-Ala-Asn-Gly-Thr-Gly-Pro-Gly-Gly-Asn-Ser-Lys-Thr-Gly-Arg-Tyr-Glu-Phe-Gly. The purified protease was toxic for mice (about 1·5 mg kgand 4·5 mg kg, intraperitoneal and intravenous LD values, respectively), and subcutaneous injection of the enzyme elicited rapid and extensive dermonecrosis.


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