KaydedilenlerDerginizi ekleyin

Dergiler / Hacettepe Journal of Biology and Chemistry / 2009 / Cilt: 37 - Sayı: 3

Histidine pseudobioaffinity separation technology: a powerful tool for the separation of antibodies

Assem ELKAK
Sayfa
169–180
Yayın Tarihi
2022-10-17
DOI
—
🏛️Bu makalenin bibliyografik verileri ve tam metin bağlantısı DergiPark üzerinden sağlanmıştır.
DergiPark Kaydı ↗
✨

Yapay Zeka Hızlı Bakış & Çıkarımlar

AI Insight
⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

This review focuses on the separation of antibodies by pseudobioaffinity separation technology on histidine grafted to different activated matrix.

📌 3 Maddede Bu Makale

🎯
Amaç & Hipotez:Vital substances derived from blood are extracted, a great deal by procedures of fractionation.
📊
Temel Bulgular & Veri: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.
💡
Sonuç & Katkı:This review focuses on the separation of antibodies by pseudobioaffinity separation technology on histidine grafted to different activated matrix.
🔬Tür:Literatür & Derleme Çalışması
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Alan Parametreleri

Abstract

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.

🔖

Bu Makaleye Atıf Yap

ELKAK, A. (2022). Histidine pseudobioaffinity separation technology: a powerful tool for the separation of antibodies. Hacettepe Journal of Biology and Chemistry, Cilt: 37 - Sayı: 3, 169–180. https://ajindex.com/articles/529330

📄 Tam Metin PDF Okuyucu

📄

PDF görüntüleyici hazırlanıyor...

Kaynakça (28)

  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
  5. Beck, O.E., Clin. Exp. Immunol., 43 (1981) 626
  6. Bird, P., Lowe, J., Stokes, R.P. Bird, A.G., Ling, N.R., Jefferis, R. J. Immunol. Methods., 71 (1984) 97
  7. Burton, D.R., Gregory, L. and Jefferis, R. Monographs Allergy, 19 (1986) 7
  8. Bueno, S.M.A., Haupt, K. and Vijayalakshmi, M.A. J. Membr. Sci., 117 (1996) 45
  9. 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
  10. Haupt, K. and Vijayalakshmi, M.A. J. Chromatogr., 644 (1993) 289
  11. Darnige, L., Legallais, C., Arvieux, J., Pitiot, O. and Vijayalakshmi, M.A. Artificial Organs, 23(9) (1999) 834
  12. Vijayalakshmi, M.A. Molecular Biotechnology, 6 (1996) 347
  13. Kohler, G. and Milstein, C. Nature, 256 (1975) 495
  14. Shimizu, F., Wang, R. and Varga, S. J. Clin. Chem., 29 (1983) 1245
  15. Yelton, D.E. and Scharff, M.D. Ann. Rev. Biochem., 50 (1981) 657
  16. Larson, S.M., Brown, J.P. and Hellston, K.E. J. Nucl. Med., 24 (1983) 123
  17. Elkak, A. and Vijayalakshmi, M.A. J. Chromatogr. Biomedical Applications, 570 (1991) 29
  18. Johansson, B.G. In Blomback, B., Hanson, L.A. (eds): Plasma Proteins., New York, Wiley, (1979) 309
  19. Pirofsky, B., Anderson, C.J., Bardana, E.J. Jr. In Alving, B.M. (ed)., Washington, DC., (1980) 15
  20. Stiehm, E.R., Ashida, E., Kim, K.S., Winston, D.J., Haas, A., Gale R.P. Ann. Intern. Med., 107 (1987) 367
  21. 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
  22. Oncley, J.L., Melin, M., Richert, D.A., Cameron, J.W., Gross, P.M. Jr. J. Am. Chem. Soc., 71 (1949) 541
  23. Polson, A., Ruiz-Bravo, C. Vox Sang, 23 (1972) 107
  24. Grabar, P. and Williams, C. Biochim. Biophys. Acta, 10 (1953) 193
  25. Mancini, G., Carbonara, A. and Heremans, F. Immunochemistry, 2 (1965) 235
  26. Elkak, A. and Vijayalakshmi, M.A. Bioseparation, 3 (1992) 47
  27. 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
  28. Quesniaux, V.F.J., Tees, R., Schreier, M.H., Wneger, R.M. and Regenmort