Histidine Pseudobioaffinity Separation Technology: a Powerful Tool for the Separation of Antibodies

Vital substances derived from blood are extracted, a great deal by procedures of fractionation. The vast progress in biotechnology and molecular biology presented a vast range of possibilities to improve these procedures. One of the major targets of biotechnologies applied to blood plasma is to produce valuable therapeutic proteins. This is done either by purification or by synthesis through microorganisms or animals. Nowadays, the procedures of purification revolve around the one developed by Cohn. Several chromatographic methods, which are based on certain physico-chemical parameters were developped and suggested. Nevertheless, the majority of these methods had limitations such as, the purity of the final product, the cost, the toxicity, the selectivity, the recovery rate following separation in order to obtain the final desired product. Introducing histidine as a ligand, in pseudobioaffinity chromatography eliminated these limitations and presented a reliable and efficient mean of separation of several molecules intended for therapeutic and medical use. This review focuses on the separation of antibodies by pseudobioaffinity separation technology on histidine grafted to different activated matrix.

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  • 1. Ratsimbazafy, V. Actualiés Pharmaceutiques, 385 (2000) 19.
  • 2. Janson, J.C. Tibtech., 2 (1984) 31.
  • 3. Wilchek, M., Miron, T. and Kohn, J. Methods in Enzymol., 104 (1984) 3.
  • 4. Vijayalakshmi, M.A. and Porath, J. J. Chromatogr., 177 (1979) 201
  • 5. Rabier, J., Vijayalakshmi, M.A. and Lambert, C. J. Chromatogr., 303 (1984) 285.
  • 6. Beck, O.E., Clin. Exp. Immunol., 43 (1981) 626.
  • 7. Bird, P., Lowe, J., Stokes, R.P. Bird, A.G., Ling, N.R., Jefferis, R. J. Immunol. Methods., 71 (1984) 97.
  • 8. Burton, D.R., Gregory, L. and Jefferis, R. Monographs Allergy, 19 (1986) 7.
  • 9. Bueno, S.M.A., Haupt, K. and Vijayalakshmi, M.A. J. Membr. Sci., 117 (1996) 45.
  • 10. Ezzedine, M. Lawny, F. and Vijayalakshmi, M.A. In Biotechnology of Blood Proteins, Ed. J.F. Stoltz and Rivat, C. INSERM/ John Libbey, 227 (1993) 115.
  • 11. Haupt, K. and Vijayalakshmi, M.A. J. Chromatogr., 644 (1993) 289.
  • 12. Darnige, L., Legallais, C., Arvieux, J., Pitiot, O. and Vijayalakshmi, M.A. Artificial Organs, 23(9) (1999) 834.
  • 13. Vijayalakshmi, M.A. Molecular Biotechnology, 6 (1996) 347.
  • 14. Kohler, G. and Milstein, C. Nature, 256 (1975) 495.
  • 15. Shimizu, F., Wang, R. and Varga, S. J. Clin. Chem., 29 (1983) 1245.
  • 16. Yelton, D.E. and Scharff, M.D. Ann. Rev. Biochem., 50 (1981) 657.
  • 17. Larson, S.M., Brown, J.P. and Hellston, K.E. J. Nucl. Med., 24 (1983) 123.
  • 18. Elkak, A. and Vijayalakshmi, M.A. J. Chromatogr. Biomedical Applications, 570 (1991) 29.
  • 19. Johansson, B.G. In Blomback, B., Hanson, L.A. (eds): Plasma Proteins., New York, Wiley, (1979) 309.
  • 20. Pirofsky, B., Anderson, C.J., Bardana, E.J. Jr. In Alving, B.M. (ed)., Washington, DC., (1980) 15.
  • 21. Stiehm, E.R., Ashida, E., Kim, K.S., Winston, D.J., Haas, A., Gale R.P. Ann. Intern. Med., 107 (1987) 367.
  • 22. Cohn, E.J., Stong L.E., Hughes, W.L. Jr., Mulford D.J. Asworth, J.N., Melin, M., Taylor, H.L. J. Am. Chem. Soc., 8 (1946) 459.
  • 23. Oncley, J.L., Melin, M., Richert, D.A., Cameron, J.W., Gross, P.M. Jr. J. Am. Chem. Soc., 71 (1949) 541.
  • 24. Polson, A., Ruiz-Bravo, C. Vox Sang, 23 (1972) 107.
  • 25. Grabar, P. and Williams, C. Biochim. Biophys. Acta, 10 (1953) 193.
  • 26. Mancini, G., Carbonara, A. and Heremans, F. Immunochemistry, 2 (1965) 235.
  • 27. Elkak, A. and Vijayalakshmi, M.A. Bioseparation, 3 (1992) 47.
  • 28. Quesniaux, V.F.J., Tees, R., Schreier, M.H., Wneger, R.M., Donatsch, P. and Regenmortel, M.H.V. In Ciclosporin Progress in Allergy (edited by Borel J.F. 38 (1986) 108.
  • 29. Quesniaux, V.F.J., Tees, R., Schreier, M.H., Wneger, R.M. and Regenmortel, M.H.V. Molec. Immunol., 24 (1987) 1159.
  • 30. Quesniaux, V.F.J., Schmitter. D., Schreier, M.H. and Regenmortel, M.H.V. Molec. Immunol., 27 (1990) 227.
  • 31. Petcher, T.J., Weber, H.P. and Ruegger, A. Helv. Chim. Acta., 59 (1986) 1480.
  • 32. Loosli, H.R., Keesler, H., Oschkinat, H., Weber, H.P., Petcher, T.J. and Widmer, A. Helv. Chem. Acta., 68 (1985) 682.
  • 33. Wenger, R.M., Payne T.G. and Schreier. M.H. Progr. Clin. Biochem. Med., 3 (1986) 159.
  • 34. Schmitter, D., Poch, O., Zeder, G., Heinrich, G.F., Kocher, H.P., Quesniaux, V.F.J. and Regenmortel, M.H.V. Mol. Immunol., 27 (10) (1990) 1029.
  • 35. Quirk, D.J. and Raines, R.T. Biophysical J., 76 (1999) 1571.
  • 36. Schultz, L.W., Quirk, D.J. and Raines, R.T. Biochemistry, 37 (1998) 8886.
  • 37. Khamashta, M.A., Hughes, G.R.Clin. Rev. Allergy, 12 (1994) 287.
  • 38. Harris, E.N., Gharavi, A.E., Boey, M.L., Patel, B.M., Mackworth-Young, C., Hughes, G.R. Lancet, 2 (1983) 1211.
  • 39. Greaves, M. Lancet, 353 (1999) 1348.
  • 40. Fehr, T., Cathomas, G., Weber, C., Fontana, A., Schaffner, A., Lupus, 10(8) (2001) 576.
  • 41. Galli, M., Finazzi, M., Barbui, T. Br J Haemat., 93(1) (1996) 1.
  • 42. Tyutulkova, S., Paul, S. Appl. Biochem. Biotech., 47 (1994) 191.
  • 43. Tyutulkova, S., Gao, Q.S., Paul, S. In Methods in Molecular Biology. Antibody Engineering Protocols, Paul, S. Edition, Humana, Totowa NJ 51 (1995) 377.
  • 44. Buchner, J., Renner, M., Lilie, H., Hin, H.J., Jaenicke, R. Biochemistry, 30 (1991) 6922.
  • 45. Shuster, A.M., Gololobov, G.V., Kvashuk, O.K., Bogomolova, A.T.E., Smirnov, I.V., Gabibov, A.G. Science, 256 (1992) 665.
  • 46. Sarath, G., De La Motte, R.S., Wagner, F.W. In Proteolytic Enzymes : A Practical approach, Beyroun, R.J., Bond, J.S. (eds) Oxford UK (1989) 25.
  • 47. Elkak, A., Bourhim, M., Coffinier, Y., Vijayalakshmi, M.A. Chromatographia, 60(3/4) (2004) 165.