Purification of Hemoglobin by Ion Exchange Chromatography in Flow-Through Mode with PEG as an Escort

References

• Bradford M. M. A rapid and sensitive method for the quantification of microgramme quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976; 72: 248–254, [PUBMED], [INFOTRIEVE]
   PubMed Web of Science ®Google Scholar
• Bruno G., Gino A. Measurement of binding of gaseous and nongaseous ligands to hemoglobin by conventional spectrophotometric procedure. Methods in Enzymology 1981; 76: 417–427
   PubMedGoogle Scholar
• Cagnon P., Godfrey B., Ladd D. Method for obtaining unique selectivities in ion-exchange chromatography by addition of organic polymers to the mobile phase. J. Chromatography 1996; 743: 51–55, [CROSSREF]
   Google Scholar
• Chang T. M. S. Red blood cell substitutes. Best Pract. Res. Clin. Haematol. 2000; 13: 651–668, [CROSSREF], [CSA]
   PubMed Web of Science ®Google Scholar
• Cheung L. C., Storm C. B., Babriel B. W. The preparation of stroma-free hemoglobin by DEAE-cellulose absorption. Anal. Biochem. 1984; 137: 481–484, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Christensen S. M., Media F., Winslow R. M., Snell S. M., Zegn A., Marini M. A. Preparation of human hemoglobin A0 for possible use as a blood substitute. J. Biochem. Biophys. Methods 1988; 17: 143–154, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   PubMedGoogle Scholar
• Cleland J. L., Randolph T. W. Mechanism of polyetheylene glycol interaction with the molten globule intermediate on the carbonic anhydrase folding pathway. J. Biol. Chem. 1992; 267: 3147–3153, [PUBMED], [INFOTRIEVE]
   PubMedGoogle Scholar
• Deloach J. R., Sheffield C. L., Spates G. E. A continuous-flow high-yield process for preparation of lipid-free hemoglobin. Anal. Biochem. 1986; 157: 191–198, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Demmer W., Nussbaumer D. Large-scale membrane adsorbers. Journal of Chromatography A 1999; 852: 73–81, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Doczi J.. Injectable Stroma Free Hemoglobin and Its Method of Manufacture. US Patent 3,991,181, 1976
   Google Scholar
• Dodge J. T., Mitchell C., Hanahan D. The preparation and characteristics of hemoglobin-free ghosts of human erythrocytes. Arch. Biochem. Biophys. 1963; 100: 119–130, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Donald J. H. A Guide to Phosphalipid Chemistry. Oxford University Press, New York 1997
   Google Scholar
• Dorman S. C., Kenny C. F., Miller L., Hirsch R. E., Harrington J. P. Role of redox potential of hemoglobin-based oxygen carriers on methemoglobin reduction by plasma component. Art. Cells, Blood Subs., and Immob. Biotech. 2002; 30(1)39–51, [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Feng X. L., Gu Z. Y., Jin Y. T., Su Z. G. Polyethylene glycol improves the purification of recombinant human tumor necrosis factor during ion exchange chromatography. Biotechnology Techniques 1998; 12(4)293–298, [CROSSREF]
   Google Scholar
• Hsia J. C. Purification of hemoglobin and modified hemoglobin by ATP-agarose affinity chromatography. J. Chromatogr. 1996; 374: 143–148
   Google Scholar
• Inada Y. Biomedical and biotechnological applications of PEG- and PM-modified proteins. Trends in Biotechnology 1995; 13: 86–91, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   PubMed Web of Science ®Google Scholar
• Ingham K. C., Busby T. F. Methods of removing polyethylene glycol from plasma fractions. Chem. Eng. Commun. 1980; 7: 315–326
   Web of Science ®Google Scholar
• Janson J. C., Ryden L. Protein Purification: Principles, High Resolution Methods, and Applications. 2nd ed. John Wiley & Sons, Inc. Publication, New York 1997; 3–41
   Google Scholar
• Lu X. L., Zhao D. X., Jin Y. T., Su Z. G. Efficient separation and purification of bovine hemoglobin using expanded bed adsorption. Journal of Chemical Industry and Engineering 2003; 54(9)1257–1263
   Google Scholar
• Mehgnin E. A., Plajura D. H., Ehshraf S.. Method of Commercial-scale Purification of Hemoglobin. RU Patent 2,145,873, February 27, 2000
   Google Scholar
• Nedjar-Arroume N., Castellane A., Guillocbon D. Stabilizing effect of water/alcohol solvents towards autoxidation of glutaraldehyde-modified haemoglobin. Biotechnol. Appl. Biochem. 1995; 21: 173, [PUBMED], [INFOTRIEVE], [CSA]
   PubMedGoogle Scholar
• Riggs A. Methods in Enzymology, E. Antonini, L. Rossi-Beradi, E. Chiancone. Academic Press, Orlando, FL 1981; Vol. 76: 5–29
   Google Scholar
• Sheffield C. L., Spates G. E., Droleskey R. E., Green R., Deloach J. R. Preparation of lipid-free human hemoglobin by dialysis and ultrafiltration. Biotechnol. Appl. Biochem. 1987; 9: 230–238, [PUBMED], [INFOTRIEVE], [CSA]
   PubMed Web of Science ®Google Scholar
• Shorr R. G., Nho K., Cho M. O.. Process for Hemoglobin Extraction and Purification. US Patent 5,264,555, November 23, 1993
   Google Scholar
• Timasheff S. N. Stabilization of protein structure by solvent additives. Stability of Protein Phamarceuticals (Part B), T. J. Ahern, M. C. Manning. Plenum Press, New York 1992
   Google Scholar
• Winslow R. M. Blood substitutes. Advanced Drug Delivery Reviews 2000; 40: 131–142, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   PubMed Web of Science ®Google Scholar
• Xue H., Zheng H., Wu X. F. Preparation of highly purified hemoglobin by affinity elution. Artif. Cells Blood Substit. Immobil. Biotechnol. 1998; 26(3)317–327, [PUBMED], [INFOTRIEVE], [CSA]
   PubMed Web of Science ®Google Scholar
• Yan S. C. B., Tuason D. N., Tuason V. B. Polyethylene glycol interferes with protein molecular weight determination by gel filtration. Anal. Biochem. 1984; 138: 137–140, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMedGoogle Scholar
• Zhao D. X., Wei X. G., Gu Z. Y., Zhang G. F., Su Z. G. Preparation of bovine lipid-free hemoglobin. Chinese Journal of Biotechnology 2002; 18(5)609–613, [PUBMED], [INFOTRIEVE]
   Google Scholar