On the appearance of Bacillus subtilis intracellular serine protease in the cell membrane and culture medium |
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Authors: | Alexander Ya Strongin Lara S Izotova Zakhar T Abramov Lidia M Ermakova Dmitrii I Gorodetsky Valentin M Stepanov |
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Institution: | (1) Institute of Genetics and Selection of Industrial Microorganisms, Dorojnaya 8, 113545 Moscow, USSR |
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Abstract: | 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 nonionic 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.Abbreviations ISP
intracellular serine protease
- ISP-A-Bsu A-50 and ISP-B-Bsu A-50
molecular forms A and B of B. subtilis A-50 intracellular serine protease, respectively
- SDS
sodium dodecyl sulfate
- PMSF
phenylmethyl sulfonylfluoride
- pNA
p-nitroanilide
- Buffer A
50 mM Tris-(hydroxymethyl)aminomethane-1 mM CaCl2 adjusted to pH 8.5 with HCl |
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Keywords: | Bacillus subtilis Proteases Serine proteases |
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