Summary
A procedure for purification of a serine alkaline proteinase from Streptomyces rimosus waste broth was developed. The procedure includes ultrafiltration, CM-Sephadex C-50 and CM-cellulose chromatography and gel filtration on Sephadex G-75. The recovery of electrophoretically pure enzyme was 25%. The enzyme is active on different protein and synthetic substrates at neutral and alkaline pHs but its activity on hemoglobin and bovine serum albumin, is optimal at pH 4.0–4.5. It has a molecular weight of 22,000 and a pI of 4.90. The enzyme is inhibited by DFP and PMSF but not by TPCK. Its substrate specificity, amino acid composition and some other properties were also determined.
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Renko, M., Pokorny, M., Vitale, L. et al. Streptomyces rimosus extracellular proteases. European J. Appl. Microbiol. Biotechnol. 11, 166–171 (1981). https://doi.org/10.1007/BF00511256
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DOI: https://doi.org/10.1007/BF00511256