[Metal proteases from Bac. subtilis].
Metal and serine proteases were separated on the biospecific sorbent. Two different, homogeneous metal proteases were obtained by rechromatography of the metal protease. Activation energies, heat stability, molecular weights, influence of inhibitors, the dependence of activity on pH and temperature were determined. Properties of two metal proteases were compared with those of literary analogs.
D001412:Bacillus subtilis / Q000201:enzymology*; D004355:Drug Stability; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D008667:Metalloproteins / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D013696:Temperature
D008667:Metalloproteins; D010447:Peptide Hydrolases
Metalloproteazy Bac. Subtilis