The Study of Escherichia coli Proteases. Intracellular Serine Protease of E. coli - an Analogue of Bacillus Proteases

References

1. Andrews P. 1964; Estimation of the molecular weight of proteins by Sephadex gel-filtration. Biochemical Journal 91:222–233
   [Google Scholar]
2. Cheng Y., Aronson A. I. 1977a; Alterations of spore coat processing and protein turnover in a Bacillus cereus mutant with a defective post-exponential intracellular protease. Proceedings of the National Academy of Sciences of the United States of America 74:1254–1258
   [Google Scholar]
3. Cheng Y., Aronson A. I. 1977b; Characterization and functions of intracellular proteases in sporulating Bacillus cereus. Archives of Microbiology 115:61–66
   [Google Scholar]
4. Davis B. J. 1964; Disc electrophoresis. II. Method and application to human serum proteins. Annals of the New York Academy of Sciences 121:404–427
   [Google Scholar]
5. Hageman J. H., Carlton B. C. 1973; Effects of mutational loss of specific intracellular proteases on the sporulation of Bacillus subtilis. Journal of Bacteriology 114:612–617
   [Google Scholar]
6. Ikenaka T., Odani S., Sakai M., Nabeshima Y., Sato S., Murao S. 1974; Amino acid sequence of an alkaline proteinase inhibitor (Streptomyces Subtilisin Inhibitor) from Streptomyces albogriseolus S-3253. Journal of Biochemistry 76:1191–1209
   [Google Scholar]
7. Izotova L. S., Gorodetsky D. I., Yanonis V. V., Baratova L. A., Belyanova L. P., Timokhina E. A., Strongin A. Ya., Stepanov V. M. 1978; Isolation of Bacillus subtilis intracellular serine protease by Gramicidin S–Sepharose 4B affinity chromatography. Bioorganicheskaya Khimiya 4:397–403 (in Russian)
   [Google Scholar]
8. Lecadet M.-M.,, Lescourret M., Klier A. 1977; Characterization of an intracellular protease isolated from Bacillus thuringiensis sporulating cells and able to modify homologous RNA polymerase. European Journal of Biochemistry 79:329–338
   [Google Scholar]
9. Lyublinskaya L. A., Belyaev S. V., Strongin A. Ya.,, Matyash L. F., Levin E. D., Stepanov V. M. 1974; A new chromogenic substrate for subtilisin. Analytical Biochemistry 62:371–376
   [Google Scholar]
10. Lyublinskaya L. A., Yakusheva L. D., Stepanov V. M. 1977; Synthesis of subtilisin peptide substrates and their analogs. Bioorganicheskaya Khimiya 3:273–279 (in Russian)
    [Google Scholar]
11. Miller C. G., Zipser D. 1977; Degradation of Escherichia coli β-galactosidase fragments in protease-deficient mutants of Salmonella typhimurium. Journal of Bacteriology 130:347–353
    [Google Scholar]
12. Miller C. G., Heiman C., Yen C. 1976; Mutants of Salmonella typhimurium deficient in an endoprotease. Journal of Bacteriology 127:490–497
    [Google Scholar]
13. Pacaud M. 1976; Purification of protease II from Escherichia coli by affinity chromatography and separation of two enzyme species from cells harvested at late log phase. European Journal of Biochemistry 64:199–204
    [Google Scholar]
14. Pacaud M., Richaud C. 1975; Protease II from Escherichia coli. Purification and characterization. Journal of Biological Chemistry 250:7771–7779
    [Google Scholar]
15. Pacaud M., Uriel J. 1971; Isolation and some properties of a proteolytic enzyme from Escherichia coli (protease I). European Journal of Biochemistry 23:435–442
    [Google Scholar]
16. Pacaud M., Sibilli L., Le Bras G. 1976; Protease I from Escherichia coli. Some physicochemical properties and substrate specificity. European Journal of Biochemistry 69:141–151
    [Google Scholar]
17. Stepanov V. M., Strongin A. Ya.,, Izotova L. S., Abramov Z. T., Lyublinskaya L. A., Ermakova L. M., Baratova L. A., Belyanova L. P. 1977a; Intracellular serine protease from Bacillus subtilis. Structural comparison with extracellular serine proteases – subtilisins. Biochemical and Biophysical Research Communications 77:298–305
    [Google Scholar]
18. Stepanov V. M., Strongin A. Ya.,, Izotova L. S., Abramov Z. T. 1977b; Intracellular proteinase of Bacillus subtilis. Acta biologica et medica germanica 36:1509–1514
    [Google Scholar]
19. Strongin A. Ya.,, Azarenkova N. M., Vaganova T. I., Levin E. D., Stepanov V. M. 1976; Visualization of leucineaminopeptidase activity after acrylamide gel electrophoresis. Analytical Biochemistry 74:597–599
    [Google Scholar]
20. Strongin A. Ya.,, Izotova L. S., Abramov Z. T., Gorodetsky D. I., Ermakova L. M., Baratova L. A., Belyanova L. P., Stepanov V. M. 1978a; Intracellular serine protease of Bacillus subtilis: sequence homology with extracellular subtilisins. Journal of Bacteriology 133:1401–1411
    [Google Scholar]
21. Strongin A. Ya.,, Izotova L. S., Abramov Z. T., Gorodetsky D. I., Stepanov V. M. 1978b; Two related structural genes coding two homologous serine proteases in the Bacillus subtilis genome. Molecular and General Genetics 159:337–339
    [Google Scholar]
22. Strongin A. Ya.,, Izotova L. S., Abramov Z. T., Gorodetsky D. I., Ermakova L. M., Stepanov V. M. 1978c; On the appearance of Bacillus subtilis intracellular serine protease in the cell membrane and culture medium. Comparison of the enzyme with other Bacillus subtilis serine proteases. Archives of Microbiology (in the Press)
    [Google Scholar]
23. Strongin A. Ya.,, Gorodetsky D. I., Kuznetsova I. A., Abramov Z. T., Yanonis V. V., Belyanova L. P., Baratova L. A., Stepanov V. M. 1979a; Intracellular serine proteinase of Bacillus subtilis strain Marburg 168. Comparison with the homologous enzyme from Bacillus subtilis strain A-50. Biochemical Journal (in the Press)
    [Google Scholar]
24. Strongin A. Ya,, Abramov Z. T., Yaroslavtseva N. G., Baratova L. A., Belyanova L. P., Stepanov V. M. 1979b; Direct comparison of the subtilisin-like intracellular protease of Bacillus licheniformis with the homologous enzymes of Bacillus subtilis . Journal of Bacteriology (in the Press)
    [Google Scholar]
25. Szulmajster J., Keryer E. 1975; Isolation and properties of thermosensitive sporulation mutants of Bacillus subtilis deficient in intracellular protease activity. In Spores VI, pp. 271–278 Edited by Gerhardt P., Sadoff H. L., Costilow R. W. Washington D. C.: American Society for Microbiology;
    [Google Scholar]