Cloning and expression of an intracellular alkaline protease gene from alkalopihilic thermoactinomyces sp. Η8682

Bioscience, Biotechnology and Biochemistry

Volumn 61, Issue 2, 1997, Pages 298-303

  Tsuchiya, Katsumi ^a   Ikeda, Ichiro ^a   Tsuchiya, Takashi ^a   Kimura, Tetsu ^a  

^a JOSAI UNIVERSITY   (Japan)

Author keywords

Alkalophilic Thermoactinomyces sp; Amino acid sequence homology; DNA sequence; Intracellular alkaline serine protease; Protein purification

Indexed keywords

EID: 0031079977     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.61.298     Document Type: Article

References (29)

1. G. M. Frost and D. A. Moss, in “Biotechnology, Vol. 7a, Enzyme Technology,” ed. by J. F. Kennedy, VCH, Weinheim, 1987, pp. 157-168.
2. O. P. Ward, in “Microbial Enzymes and Biotechnology,” ed. by W. H. Forgarty, Applied Science Publishers, London, 1983, pp. 251-317.
3. W. Peczynska-Czoch and M. Mordarski, in “Actinomyces in Biotechnology,” ed. by M. Goodfellow, S. T. Williams, and M. Moedarshi, Academic Press, New York, 1988, pp. 246-253.
4. K. Florikoshi, in “Microorganisms in Alkaline Environments,” YCH, Weinheim, 1991, pp. 187-193.
5. H. Takami, T. Akiba, and K. Horikoshi, Appl. Microbiol. Biotechnol., 30, 120-124 (1992).
6. K. Tsuchiya, Y. Nakamura, H. Sakashita, and T. Kimura, Biosci. Biotech. Biochem., 56, 246-250 (1992).
7. H. Takami, T. Akiba, and K. Horikoshi, Biosci. Biotech. Biochem., 56, 510-511 (1992).
8. H. Saito and K. Miura, Biochim. Biophys. Acta, 72, 619-629 (1963).
9. H. C. Birnboim and J. Doly, Nucl. Acids Res., 7, 1513-1523 (1979).
10. D. Hanahan, J. Mol. Biol., 166. 557-580 (1980).
11. J. Sambrook, E. F. Fritsh, and T. Maniatis, in “Molecular Cloning: A Laboratory Manual,” 2nd Ed., ed. by Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1989.
12. S. Henikoff, Gene, 28, 351-359 (1984).
13. M. Hattori and Y. Sakaki. Anal. Biochem., 152, 232-238 (1986).
14. F. Sanger, S. Nicklen, and A. R. Coulson, Proc. Natl. Acad. Sei. U.S.A., 74, 5463-5467 (1984).
15. U. K. Laemmli, Nature, 227, 680-685 (1970).
16. M. M. Bradford, Anal. Biochem., 72, 248-254 (1976).
17. A. P. Feinberg and B. Vogelstein, Anal. Biochem., 132, 6-13 (1983); Anal. Biochem., 137, 266-267 (1984).
18. E. M. Southern, J. Mol. Biol., 98, 503-517 (1975).
19. J. Shine and L. Dalgarno, Proc. Natl. Acad. Sei. U.S.A.,11,1342-1346 (1974).
20. S. Adhya and M. Gottesman, Ana. Rev. Biochem.,47, 967-996(1978).
21. I. Tinoco, Jr., P. N. Borer, B. Dengler, M. D. Levine, O. C. Uhlenbeck, D. M. Crothers, and J. Gralla, Nature New Biol., 246, 40-41 (1973).
22. S. M. Sheen and R. L. Switzer, J. Bacterial., 172, 473-476 (1990).
23. Y. Koide, A. Nakamura, T. Uozumi, and T. Beppu, J. Bacteriol., 167, 110-116 (1988).
24. S. Takekawa, N. Uozumi, N. Tsukagoshi, and S. Udaka, J. Bacteriol., 173, 6820-6825 (1991).
25. H. Takami, T. Kobayashi, R. Aono, and K. Horikoshi, Appl. Microbiol. Biotech., 38, 101-108 (1992).
26. H. Takami, T. Kobayashi, M. Kobayashi, M. Yamamoto, S. Nakamura, R. Aono and K. Horikoshi, Biosci. Biotech. Biochem., 56, 1455-1460 (1992).
27. R. Kaneko, N. Koyama, Y. C. Tsai, R. Y. Juang, K. Yoda, and M. Yamasaki, J. Biochem., 171, 5232-5236 (1989).
28. N. Vasantha, L. D. Thomson, C. Phodes, and C. Banner, J. Bacteriol., 159, 811-819 (1984).
29. B. Meloun, M. Baudys, V. Kostka, G. Hausdorf, and C. Frommel, FEBS Lett., 183, 195-200 (1985).