Purification and characterization of a novel protease from culture filtrates of a Streptomyces sp

Abstract A fibrinolytic protease has been isolated from Streptomyces sp. culture filtrate by successive chromatography on Mono S and Sephadex G50. The purified protease had a molecular mass of 33 kDa and had an isoelectric point of 6.7. It showed a sharp pH optimum at 7.8 with maximal protease activ...

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Veröffentlicht in:	FEMS microbiology letters 1996-08, Vol.141 (2-3), p.213-220
Hauptverfasser:	Bono, Françoise, Savi, Pierre, Tuong, Anne, Maftouh, Mohamed, Pereillo, Jean-Marie, Capdevielle, Joel, Guillemot, Jean-Claude, Maffrand, Jean-Pierre, Herbert, Jean-Marc
Format:	Artikel
Sprache:	eng
Schlagworte:	a1-antitrypsin Amino acid composition Amino Acid Sequence Amino acids Bacteriology Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Chromatography, Gel Chromatography, Ion Exchange Chymotrypsin Dithiothreitol Endopeptidases - chemistry Endopeptidases - isolation & purification Ethylenediaminetetraacetic acids Fibrin Fibrinolysis Filtrate Fluorides Fundamental and applied biological sciences. Psychology Fungi Isoelectric Point Metabolism. Enzymes Microbiology Mission oriented research Molecular Sequence Data Organic chemistry Phenylmethylsulfonyl fluoride Physiology and metabolism Protease Protease Inhibitors - metabolism Proteinase Purification Serine Sodium dodecyl sulfate Sodium lauryl sulfate Soybeans Streptomyces Streptomyces - enzymology Streptomyces sp Substrate Specificity Substrates Trypsin Trypsin inhibitors
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