Physical and kinetic effects on introduction of various linker regions in β-galactosidase/galactose dehydrogenase fusion enzymes

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1293, Issue 1, 1996, Pages 154-160

  Carlsson, Helén ^a   Ljung, Sarah ^a   Bülow, Leif ^a  

^a Dept of Pure and Appl Biochemistry ^*  (Sweden)

Author keywords

Bifunctional enzyme; E. coli; Galactose dehydrogenase; Gene fusion; Linker region; Galactosidase

Indexed keywords

BETA GALACTOSIDASE; GALACTOSE DEHYDROGENASE; HYBRID PROTEIN;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE FUSION; GROWTH RATE; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; STRUCTURE ACTIVITY RELATION;

ESCHERICHIA COLI;

EID: 0029887939     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/0167-4838(95)00240-5     Document Type: Article

References (28)

1. Bülow, L. and Mosbach, K. (1991) Trends Biotechnol. 9, 226-231.
2. Bülow, L. (1987) Eur. J. Biochem. 163, 443-448.
3. Ljungcrantz, P., Carlsson, H., Månsson, M.-O., Buckel, P., Mosbach, K. and Bülow, L. (1989) Biochemistry 28, 8786-8792.
4. Lindbladh, C., Rault, M., Small, W.C., Mosbach, K., Bülow, L., Evans, C. and Srere, P.A. (1994) Biochemistry 33, 11692-11698.
5. Lindbladh, C., Persson, M., Bülow, L. and Mosbach, K. (1992) Eur. J. Biochem. 204, 241-247.
6. Sakaki, T., Kominami, S., Takemori, S., Ohkawa, H., Akiyoshishibata, M. and Yabusaki, Y. (1994) Biochemistry 33, 4933-4939.
7. Carlsson, H., Ljungcrantz, P., Bülow, L. and Mosbach, K. (1992) Biotechnol. Lett. 14, 439-444.
8. Slilaty, S.N., Quellet, M., Fung, M. and Shen, S.-H. (1990) Eur. J. Biochem. 194, 103-108.
9. Maniatis, T., Fritsch, E. and Sambrook, J. (1989) Molecular Cloning. A Laboratory Manual, 2nd Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
10. Rüther, U., Koenen, M., Otto, K. and Müller-Hill, B. (1981) Nucleic Acids Res. 9, 4087-4097.
11. Miller, J.H. (1972) Experiments in Molecular Genetics, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
12. Fowler, A.V. and Zabin, I. (1983) J. Biol. Chem. 258, 14354-14358.
13. Laemmli, U.K. (1970) Nature (London) 227, 680-685.
14. Keleti, K. (1986) Basic Enzyme Kinetics, Akademiai Kiado, Budapest, Hungary.
15. Easterby, J.S. (1981) Biochem. J. 199, 155-161.
16. Sassenfeld, H.M. (1990) Trends Biotechnol. 8, 88-93.
17. Lilius, G., Persson, M., Bülow, L. and Mosbach, K. (1991) Eur. J. Biochem. 198, 499-504.
18. Zalkin, H., Paluh, J.L., van Cleemput, M., Moye, W. and Yanofsky, C. (1984) J. Biol. Chem. 259, 3985-3992.
19. Chang, S.-I. and Hammes, G.G. (1990) Acc. Chem. Res. 23, 363-369.
20. Crawford, I.P., Clarke, M., van Cleemput, M. and Yanofsky, C. (1987) J. Biol. Chem. 262, 239-244.
21. Galakatos, N.G. and Walsh, C.T. (1989) Biochemistry 28, 8167-8174.
22. Argos, P. (1990) J. Mol. Biol. 211, 943-958.
23. Hellebust, H., Murby, M., Abrahamsén, L., Uhlén, M. and Enfors, S.-O. (1989) Bio/Technology 7, 165-168.
24. Jagusztynkrynicka, E.K., Clarkcurtiss, J.E. and Curtiss, R. (1993) Infect. Immun. 61, 1004-1015.
25. Curtis, B.M., Williams, D.E., Broxmeyer, H.E., Dunn, J., Farrah, T., Jefferey, E., Clevenger, W., DeRoos, P., Martin, U., Friend, D., Craig, V., Gayle, R., Price, V., Cosman, D., March, C.J. and Park, L.S. (1991) Proc. Natl. Acad. Sci. USA 88, 5809-5813.
26. Rock, F., Everett, M. and Klein, M. (1992) Protein Eng. 5, 583-591.
27. Huber, R.E. and Brockbank, R.L. (1987) Biochemistry 26, 1526-1531.
28. Jacobson, R.H., Zhang, X.-J., Dubose, R.F. and Matthews, B.W. (1994) Nature 369, 761-766.