Abstract
An ion exchange chromatography process was developed to separate the main protein fractions of bovine blood plasma using a composite material, Q-HyperD resin, and a gel material, DEAE-Sepharose. The experiments were carried out at semipreparative scale. It was necessary to establish analytical methods of electrophoresis and HPLC to identify the fractionated proteins. Results show that these materials are able to adequately fractionate different protein groups from the raw blood plasma. This method may be used to avoid chemical fractionation using agents such as ethanol or PEG and, thus, decrease protein denaturation of the different fractions to be used for research or pharmaceutical purposes. The Q-HyperD resin presents a better retention capacity for plasma protein than DEAE-Sepharose under the experimental conditions employed.
Similar content being viewed by others
References
Linden G, Lorient D (1994) Biochimie-Agroindustrielle. Masson, Paris, France, pp 230–237
Ockerman HW, Hansen CL (1988) Animal by-product processing. Ellis Horwood, Chichester, England, pp 239–252
Rendueles M, Moure F, Fernández A, Díaz M (1996) Preliminary studies on the processing of slaughter-house blood for protein recovery. Resource Environ Biotechnol 1:193–206
Gras J (1983) Plasma proteins. Lims, London, England, pp 69–70
Burnouf T (1995) Chromatography in plasma fractionation: benefits and future trends. J Chromatogr B 664:3–15
Matsumo R, Nakanishi K, Yamamoto S (1988) Ion exchange chromatography of proteins. Marcel Dekker, New York
Cuelli G, Tayot JL (1986) Ion exchange as a production technique for proteins. World Biotech Rep 1:141–160
Boschetti E, Guerrier L, Girot P, Horvath J (1995) Preparative high-performance liquid chromatographic separation of proteins with HyperD ion-exchange supports. J Chromatogr B 664:225–231
Goheen SC, Hilsenbeck JL (1998) High-performance ion-exchange chromatography and adsorption of plasma proteins. J Chromatogr A 816:89–96
Gerberding SJ, Byers CH (1998) Preparative ion-exchange chromatography of proteins from dairy whey. J Chromatogr A 808:141–151
Tishchenko GA, Bleha M, Skvor J, Bostik T (1998) Effect of salt concentration gradient on separation of different types of specific immunoglobulins by ion-exchange chromatography on DEAE cellulose. J Chromatogr B 706:157–166
Curling JM (1980) Albumin purification by ion exchange chromatography. In: Curling JM (ed) Methods of plasma protein fractionation. Academic Press, London, pp 77–90
Andrews A (1981) Electrophoresis: theory, techniques and biochemical and clinical applications. Clarendon Press, London, p 203
Roitt I, Brostoff J, Male D (1991) Immunology. Gower Medical Publishing, London, pp 5.1–5.12
Josic D, Horn H, Schulz P, Schwinn H, Britsch L (1998) Size exclusion chromatography of plasma proteins with high molecular masses. J Chromatogr A 796:289–298
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Moure, F., Rendueles, M. & Díaz, M. Bovine plasma protein fractionation by ion exchange chromatography. Bioprocess Biosyst Eng 27, 17–24 (2004). https://doi.org/10.1007/s00449-004-0372-2
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00449-004-0372-2