On the appearance of Bacillus subtilis intracellular serine protease in the cell membrane and culture medium. Comparison of the enzyme and other Bacillus subtilis serine proteases.
While about 80% of the cell-bound intracellular serine protease of Bacillus subtilis A-50 have been recovered in the soluble fraction upon disruption of cells, the rest of the enzyme was found to be associated with the membrane fraction. Soluble cytoplasmic intracellular serine protease, as well as membrane-bound serine protease liberated by non-ionic detergent treatment, have been isolated in a pure state and shown to be identical. The same protease might also be found extracellularly, due presumably to cell lysis or altered membrane permeability. Intracellular serine protease of Bacillus subtilis A-50 was clearly related to Bacillus subtilis serine proteases W1 and bacillopeptidase F described as extracellular enzymes.
D000596:Amino Acids / Q000032:analysis; D001412:Bacillus subtilis / Q000187:drug effects / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D002463:Cell Membrane Permeability / Q000187:drug effects; D003593:Cytoplasm / Q000201:enzymology; D010450:Endopeptidases / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity; D013501:Surface-Active Agents / Q000494:pharmacology
D000596:Amino Acids; D001426:Bacterial Proteins; D013501:Surface-Active Agents; D010450:Endopeptidases