Dissolved oxygen concentration affects the accumulation of HIV-1 recombinant proteins in Escherichia coli

Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

Volumn 80, Issue 2, 1999, Pages 107-120

  Qoronfleh, M Walid ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Dissolved oxygen; Escherichia coli; Heterologous gene expression; HIV 1 proteins; Recombinant proteins

Indexed keywords

GAG PROTEIN; OXYGEN; RECOMBINANT PROTEIN; VIRUS ENVELOPE PROTEIN;

AEROBIC METABOLISM; ARTICLE; BACTERIAL GROWTH; CELL DENSITY; ESCHERICHIA COLI; FERMENTATION; GENE EXPRESSION; GENETIC RECOMBINATION; HUMAN IMMUNODEFICIENCY VIRUS 1; NONHUMAN; OXYGEN SATURATION; PROTEIN SYNTHESIS; REGULATORY MECHANISM;

CLONING, MOLECULAR; CULTURE MEDIA; ESCHERICHIA COLI; FERMENTATION; GENE PRODUCTS, ENV; HIV CORE PROTEIN P24; HIV ENVELOPE PROTEIN GP41; HIV-1; HUMANS; KINETICS; OXYGEN; RECOMBINANT PROTEINS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0032813271     PISSN: 02732289     EISSN: None     Source Type: Journal    
DOI: 10.1385/ABAB:80:2:107     Document Type: Article

References (44)

1. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K. (1994), Current Protocols in Molecular Biology, vol. 2, Wiley, New York.
2. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989), Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
3. Lee, S. Y. (1996), Trends Biotechnol. 14, 98-105.
4. Knorre, W. A., Deckwer, W. D., Kroz, D., Pohl, H. D., Riesenberg, D., Ross, A., Sanders, E., and Schulz, V. (1991), Ann. NY Acad. Sci. 646, 300-306.
5. McNeil, B. and Harvey, L. M. (1990), Fermentation: A Practical Approach, IRL, Oxford, England.
6. Norris, J. R. and Ribbons, D. W. (1970), Methods in Microbiology, Academic, London, UK.
7. Yee, L. and Blanch, H. W. (1992), Biotechnol. NY 10, 1550-1556.
8. Cutayar, J. M. and Poillon, D. (1989), Biotechnol. Lett. 11, 155-160.
9. Arcuri, E. J., Turner, K., Sharr, D., and Okita, B. (1988), SIM News 4, 33.
10. Li, X., Robbins, J. W., Jr., and Taylor, K. B. (1992), J. Indust. Microbiol. 9, 1-10.
11. Yamada, A., Ziese, M. R., Young, J. F., Yamada, Y. K., and Ennis, F. A. (1985), J. Exp. Med. 162, 663-674.
12. Stebbins, J., Deckman, I. C., Richardson, S. B., and Debouck, C. (1996), Anal. Biochem. 242, 90-94.
13. Chiang, C. S., Grove, T., Cooper, M., Cuan, J., Kowalski, A., Parcells, K., Tsunokawa, M., Rosenberg, M., Arcuri, E., and Franklin, S. (1989), Clin. Chem. 35, 946-952.
14. Zabriskie, D. W., Wareheim, D. A., and Polansky, M. J. (1987), J. Indust. Microbiol. 2, 87-95.
15. Scorer, C. A., Carrier, M. J., and Rosenberg, R. F. (1991), Nucl. Acid Res. 19, 3511-3516.
16. Okita, B., Arcuri, E., Turner, A., Sharr, D., Del Tito, B., Swanson, J., Shatzman, A., and Zabriskie, D. (1989), Biotechnol. Bioeng. 34, 854-862.
17. Heitzer, A., Mason, C. A., Snozzi, M., and Hamer, G. (1990), Arch. Microbiol. 155, 7-12.
18. Zabriskie, D. W. and Arcuri, E. J. (1986), Enzyme Microbiol. Technol. 8, 706-717.
19. Laemmli, U. K. (1970), Nature 227, 680-685.
20. Ng, V. L., Chiang, C. S., Debouck, C., McGrath, M. S., Grove, T. H., and Mills J. (1989), J. Clin. Microbiol. 27, 977-982.
21. Clark, T. A., Hesketh, T., and Seddon, T. (1985), Biotechnol. Bioeng. 27, 1507.
22. Gleiser, I. E. and Bauer, S. (1981), Biotechnol. Bioeng. 23, 1015.
23. Wang, D. I. C., Cooney, C. L., Demain, A. L., Dunnill, P., Humphery, A. E., and Lilly, M. M. (1978), in Fermentation and Enzyme Technology, Wiley, New York.
24. Khosravi, M., Ryan, W., Webster, D. A., and Stark, B. C. (1990), Plasmid 23, 138-143.
25. Chen, W., Graham, C., and Ciccarelli, R. B. (1997), J. Indust. Microbiol. Biotechnol. 18, 43-48.
26. Hellmuth, K., Korz, D. J., Sanders, E. A., and Deckwer, W. D. (1994), J. Biotechnol. 32, 289-298.
27. Khosla, C. and Baily, J. E. (1988), Nature 331, 633-635.
28. Sakamoto, S., Terada, I., Iijima, M., Matsuzawa, H., and Ohta, T. (1994), Appl. Microbiol. Biotechnol. 42, 569-574.
29. Nakagawa, S., Oda, H., and Anazawa, H. (1995), Biosci. Biotechnol. Biochem. 59, 2263-2267.
30. Herber, W. K., Baily, F. J., Carty, C. E., Heimbach, J. C., and Maigetter, R. Z. (1991), Appl. Microbiol. Biotechnol. 36, 149-152.
31. Chang, L. L., Hwang, L. Y., Hwang, C. F., and Mou, D. G. (1991), Ann. NY Acad. Sci. 646, 259-272.
32. Jung, G., Denefle, P., Becquart, J., and Mayaux, J. F. (1988), Ann. Inst. Pasteur Microbiol. 139, 129-146.
33. Bailey, F. J., Blankenship, J., Condra, J. H., Maigetter, R. Z., and Ellis, R. W. (1987), J. Indust. Microbiol. 2, 47-52.
34. Smith, M. W. and Neidhardt, F. C. (1983), J. Bacteriol. 154, 344-350.
35. Spiro, S. and Guest, J. R. (1991), Trends Biochem. Sci. 16, 310-314.
36. Gunsalus, R. P. and Park, S. J. (1994), Res. Microbiol. 145, 437-450.
37. Park, S. J., Chao, G., and Gunsalus, R. P. (1997), J. Bacteriol. 179, 4138-4142.
38. Chao, G., Shen, J., Tseng, C. P., Park, S. J., and Gunsalus, R. P. (1997), J. Bacteriol. 179, 4299-4304.
39. Jyothirmai, G. and Mishra, R. K. (1994), FEBS Lett. 340, 189-192.
40. Wang, J. C. and Lynch, A. S. (1993), Curr. Opin. Genet. Dev. 3, 764-768.
41. Dixon, R. A., Henderson, N. C., and Austin, S. (1988), Nucl. Acid Res. 16, 9933-9946.
42. Fu, J., Tonga, A. P., Shuler, M. L., and Wilson, D. B. (1992), Biotechnol. Prog. 8, 340-346.
43. Modi, R. I., Castílla, L. H., Puskas-Rozsa, S., Helling, R. B., and Adams, J. (1992), Genetics 130, 241-249.
44. Andersson, L., Yang, S., Neubauer, P., and Enfors, S. O. (1996), J. Biotechnol. 46, 255-263.