Imidazole - A New Ligand for Metal Affinity Precipitation: Precipitation of Kunitz Soybean Trypsin Inhibitor Using Cu(II)-Loaded Copolymers of 1-Vinylimidazole with N-Vinylcaprolactam or N-Isopropylacrylamide

Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

Volumn 68, Issue 1-2, 1997, Pages 121-133

  Galaev, I Yu ^a   Kumar, A ^b   Agarwal, R ^b   Gupta, M N ^b   Mattiasson, B ^a  

^a LUND UNIVERSITY   (Sweden)

^b INDIAN INSTITUTE OF TECHNOLOGY DELHI   (India)

Author keywords

Immobilized metal affinity precipitation; Kunitz soybean inhibitor; Poly(N isopropylacrylamide)

Indexed keywords

GLYCINE MAX;

EID: 1842767050     PISSN: 02732289     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02785985     Document Type: Article

References (29)

1. Sulkowski, E. (1985), Trends Biotechnol. 3, 1-7.
2. Arnold, F. H. (1991), Bio/Technology 9, 151-156.
3. Gupta, M. N. and Mattiasson, B. (1994), in Highly Selective Separations in Biotechnology, Street, G., ed., Blackie Academic & Professional, London, pp. 7-33.
4. Porath, J. (1992), Protein Expression Purific. 3, 263-281.
5. Van Dam, M. E., Wuenchell, G. E., and Arnold F. H. (1989), Biotechnol. Appl. Biochem. 11, 492-502.
6. Lilius, G., Persson, M., Bülow, L., and Mosbach, K. (1991), Eur. J. Biochem. 198, 499-504.
7. Agarwal, R. and Gupta, M. (1994), Biotechnol. Techniques 8, 655-658.
8. Galaev, I. Yu. and Mattiasson, B. (1993), Biotechnol. Bioeng. 41, 1101-1106.
9. Yamamoto, M. and Ikenaka, T. (1967), J. Biochem. (Tokyo) 62, 141-149.
10. Erlander, B. F., Kokowsky, N., and Cohen, W. (1961), Arch. Biochem. Biophys. 95, 271-278.
11. Bradford, M. M. (1976), Anal. Biochem. 72, 248-254.
12. Hames, B. D. (1986), in Gel Electrophoresis of Proteins: a Practical Approach, Hames, B. D. and Rickwod, D. eds., IRL Press, Oxford, pp. 1-86.
13. Galaev, I. Yu. and Mattiasson, B. (1992), Biotechnol. Techn. 6, 353-358.
14. Galaev, I. Yu. and Mattiasson, B. (1993), Enzyme Microb. Technol. 15, 354-366.
15. Porath, J. and Olin, B. (1983), Biochemistry 22, 1621-1630.
16. Kumar, A., Agarwal, R., Batra, R., and Gupta M. N. (1994), Biotechnol. Techniques 8, 651-654.
17. Freed, R. C. and Ryan, D. (1980), Biochim. Biophys. Acta. 624, 562-572.
18. Fratalli, V. and Steiner, R. F. (1968), Biochemistry 7, 521-530.
19. Liu, K.-J. and Gregor, H. P. (1965), J. Phys. Chem. 69, 1252-1259.
20. Todd, R. J., Johnson, R. D., and Arnold, F. (1994), J. Chromatogr. 662, 13-26.
21. Gold, D. H. and Gregor, H. P. (1960), J. Phys. Chem. 64, 1464-1467.
22. Verweij, P. D., Sital, S., Haanepen, M. J., Driessen, W. L., and Reedijk, J. (1993), Eur. Polym. J. 29, 1603-1614.
23. Bueno, S. M. A., Haupt, K., and Vijayalakshmi, M. A. (1995), J. Chromatogr. 667, 57-67.
24. El-Kak, A., Manjini, S., and Vijayalakshmi, M. A. (1992), J. Chromatogr. 604, 29-37.
25. Millot, M. C., Sebille B., Halli, A., Hommel, H., and Legrand, A. P. (1993), Chromatographia 37, 584-592.
26. Millot, M. C., Hervé, F., and Sebille, B. (1995), J. Chromatogr. 664, 55-67.
27. Hutchens, T. W., Nelson, R. W., Li, C. M., and Yip, T.-T. (1992), J. Chromatogr. 604, 125-132.
28. Hutchens, T. W. and Yip, T.-T. (1992), J. Chromatogr. 604, 133-141.
29. ChromBook (1996), Merk KGaA, Darmstadt, Germany, pp. 239-273.