Chromatography of proteins and peptides on sephadex ion‐exchangers: Dependence of the resolution on the elution schedule

Novotný, Jiří

doi:10.1016/0014-5793(71)80261-2

Cited by 16 publications

(2 citation statements)

References 7 publications

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“…trifugation (3000 rpm, 15 min), and then barium ion, remaining in the supernatant solution, was titrated with EDTA Various proteins are separated or purified by chromatogra-solution prepared with the Michaelis buffer of pH 11.0 by phy using ion exchange Sephadexes (1,2). Then attention use of phthalein complexone as a indicator.…”

Section: Introductionmentioning

confidence: 99%

Electrophoretic Light Scattering Study of Sodium Dextran Sulfate–Lysozyme Complex

Yamaguchi

Hachiya

Moriyama

et al. 1996

Journal of Colloid and Interface Science

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Section: Introductionmentioning

confidence: 99%

Electrophoretic Light Scattering Study of Sodium Dextran Sulfate–Lysozyme Complex

Yamaguchi

Hachiya

Moriyama

et al. 1996

Journal of Colloid and Interface Science

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“…The protein peak position and peak width depend on the slope of the gradient in ionexchange chromatography (Novotny, 1971;Kawasaki and Bemardi, 1970;Kato et al, 1982;Luo and Hsu, 1997).…”

Section: )mentioning

confidence: 99%

Enhancing chromatographic separations of recombinant proteins from canola extracts by genetic design and characterization of protein binding regions

Zhang

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Introduction Materials and Methods Results and Discussion Conclusions Acknowledgment Literature Cited 101 CHAPTER 4. PREDICTION OF GENETICALLY ENGINEERED PROTEIN RETENTION IN GRADIENT ELUTION CHROMATOGRAPHY BY THE ISOCRATIC ELUTION CHARACTERISTICS Abstract Introduction Theoretical Framework Materials and Methods V Results and Discussion 112 Conclusions 123 Acknowledgment 123 List of Symbols Literature Cited CHAPTER 5. SUrrABILITY OF IMMOBILIZED METAL

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Ion exchange chromatography of proteins—predictions of elution curves and operating conditions. II. Experimental verification

Yamamoto

Nakanishi

Matsuno

et al. 1983

Biotech & Bioengineering

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The applicability and validity of the model developed in Part I were confirmed experimentally. In this article, various proteins were eluted both by stepwise and linear gradient elution on DEAE ion exchangers under a variety of experimental conditions. Adsorption isotherms were measured as a function of ionic strength in batch experiments. The moment method was employed for the determination of various parameters such as the gel-phase diffusion coefficient and the longitudinal dispersion coefficient. By use of these parameters and the experimentally measured ionic strength of the peak position, the number of plates was determined according to the method described in Part I. Theoretical elution curves were calculated with the experimentally measured adsorption equilibria and the number of plates. Good agreement was observed between theory an experiments. Various factors affecting the separation were investigated. It was found that the effect of the number of plates for salts, N'(p), was negligible except the case of stepwise elution of high ionic strength buffer. When elution curves were symmetrical, the widths of the elution curves were inversely proportional to the square root of the number of plates of proteins, N(p), as in other chromatographic techniques. A simple graphical method for prediction of the peak position in linear gradient elution described in Part I was found applicable when the elution curves were symmetrical. A useful correlation of prediction of the peak width in a linear gradient elution was proposed on the basis of the approximate solution derived in Part I of this study. This graphical method and correlation permit easy prediction of the peak position and peak width in linear gradient elution in the case of symmetrical elution curves.

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Chromatography of proteins and peptides on sephadex ion‐exchangers: Dependence of the resolution on the elution schedule

Cited by 16 publications

References 7 publications

Electrophoretic Light Scattering Study of Sodium Dextran Sulfate–Lysozyme Complex

Electrophoretic Light Scattering Study of Sodium Dextran Sulfate–Lysozyme Complex

Enhancing chromatographic separations of recombinant proteins from canola extracts by genetic design and characterization of protein binding regions

Ion exchange chromatography of proteins—predictions of elution curves and operating conditions. II. Experimental verification

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