By Csaba Horváth and Leslie S. Ettre (Eds.)
content material: Chromatographic separations in biotechnology / John Frenz --
non-stop purification of proteins by way of selective nonadsorptive preparative chromatography / T.K. Nadler and F.E. Regnier --
Ion-exchange displacement chromatography of proteins : theoretical and experimental stories / Steven M. Cramer and Clayton A. Brooks --
approach chromatography in creation of recombinant items / Walter F. Prouty --
Preparative reversed-phase pattern displacement chromatography of peptides / R.S. Hodges ... [et al.] --
Displacement : chromatographic focus regulate / Jana Jacobson --
Quantitative monosaccharide research of glycoproteins : high-performance liquid chromatography / R. Reid Townsend --
Separation of glucose oxidase isozymes from Penicillium amagasakiense by means of ion-exchange chromatography / Henryk M. Kalisz and Rolf D. Schmid --
research of microsomal cytochrome P-450 styles : speedy protein liquid chromatography with ion-exchange and immobilized steel affinity desk bound stages / P.H. Roos --
Monosaccharide compositional research of Haemophilus influenzae kind b conjugate vaccine : technique for in-process research / Charlotte C. Yu Ip and William J. Miller --
Zirconium oxide established helps for biochromatographic functions / P.W. Carr ... [et al.] --
Preparative reversed-phase chromatography of proteins / Geoffrey B. Cox.
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Extra info for Chromatography in Biotechnology
Separation o f those closely related species can require high resolution techniques. Chromatography can provide that high resolution step and has been a vital tool i n bringing human insulin to the marketplace (2,10,12). It offers an excellent choice o f separation techniques that take advantage o f subtle differences i n proteins based on charge (ion exchange), size, and hydrophobicity (reversed phase and hydrophobic interaction). Since chromatographic purification involves interaction o f a part o f the protein molecule with the resin surface and usually a limited number o f points on the protein are involved i n that interaction, chromatography can be exquisitely sensitive to changes altering any o f those sites (12).
Chromatogr. 1977, 135, 511513. 24. Stringham, R. W. Selective Non-Adsorption Preparative Chromatography of Proteins; Ph. D. Thesis, Purdue University, West Lafayette, IN 1989. 25. Stringham, R. ; Grott, A. E . ; Regnier, F. Ε. Prep. Chromatogr. 1989, 1, 179-193. 26. Anicetti, V. ; Nikelly, J. G. ; ACS Symposium Series 434, American Chemical Society, Washington, DC, 1990, pp 113-126. 27. Fulton, S. ; Afeyan, Ν. ; Gordon, N. F. J. Chromatogr. 1991, 547, 452-456. 28. Afeyan, Ν. ; Fulton, S. ; Regnier, F.
ACS Symposium Series 427, American Chemical Society, Washington, DC 1990, 427, pp 118-138. 22. ; Karger, B. L. J. Am. Chem. Soc. 1988, 110, 1978-1979. 23. ; Marino, G. J. Chromatogr. 1977, 135, 511513. 24. Stringham, R. W. Selective Non-Adsorption Preparative Chromatography of Proteins; Ph. D. Thesis, Purdue University, West Lafayette, IN 1989. 25. Stringham, R. ; Grott, A. E . ; Regnier, F. Ε. Prep. Chromatogr. 1989, 1, 179-193. 26. Anicetti, V. ; Nikelly, J. G. ; ACS Symposium Series 434, American Chemical Society, Washington, DC, 1990, pp 113-126.
Chromatography in Biotechnology by Csaba Horváth and Leslie S. Ettre (Eds.)