[Serine proteases from Bac. subtilis].
Using biospecific adsorbent and subsequent gel-filtration of Sephadex G-75 three fractions of serine proteases (I--III) having different physicochemical properties were isolated from Bac. subtilis. The first protease had molecular weight of 23000--24000 (pH optimum 6,5, activation energy 16,6 ccal/mol. The second one had molecular weight of 29000, pH optimum 11,0, activation energy 14,4 ccal/mol. The third protease was a mixture of proteases with average molecular weights 26000 and pH optima at 7,0, 8,5 and 11,0.
D001412:Bacillus subtilis / Q000201:enzymology*; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D013816:Thermodynamics
D046911:Macromolecular Substances; D010447:Peptide Hydrolases
Serinovye proteazy Bacillus subtilis