Methods of protein purification and recovery

Details Methods of protein purification and recovery Methods of protein purification and recovery

2001-10-25

2009-06-09

Saoud, Christine J (Department: 1647)

Drug, bio-affecting and body treating compositions

Lymphokine

Interferon

C424S085100, C530S351000

Reexamination Certificate

active

07544354

ABSTRACT:
Improved methods for purification and recovery of interferon-beta (IFN-β) and compositions comprising substantially monomeric IFN-β are provided. In one purification method, substantially purified IFN-β or variant thereof is precipitated and then dissolved in a guanidine hydrochloride (HCl) solution. Renaturation of the protein occurs by dilution with a suitable buffer. A similar purification method absent the precipitation step is also provided. Following renaturation of the IFN-β, residual guanidine HCl is removed by diafiltration or dialysis with a pharmaceutically acceptable buffer to prepare pharmaceutical compositions comprising substantially monomeric IFN-β.

REFERENCES:
patent: 4462940 (1984-07-01), Hanisch et al.
patent: 4816440 (1989-03-01), Thomson
patent: 4894330 (1990-01-01), Hersheson et al.
patent: 4931543 (1990-06-01), Halenbeck et al.
patent: 4992271 (1991-02-01), Fernandes et al.
patent: 5004605 (1991-04-01), Hershenson et al.
patent: 5162507 (1992-11-01), Wolfe et al.
patent: 5183746 (1993-02-01), Shaked et al.
patent: 5643566 (1997-07-01), Hanisch et al.
patent: 5702699 (1997-12-01), Hanisch et al.
patent: 6887462 (2005-05-01), Shirley et al.
patent: 7371373 (2008-05-01), Shirley et al.
patent: 7399463 (2008-07-01), Shirley et al.
patent: 0 217 645 (1987-04-01), None
patent: 0 270 799 (1988-06-01), None
patent: 0 360 937 (1990-04-01), None
patent: 0 215 658 (1994-06-01), None
patent: 9 306 706 (1993-07-01), None
patent: WO 95/31479 (1995-11-01), None
patent: WO 98/27211 (1998-06-01), None
patent: WO 02/080976 (2002-10-01), None
The Merck Index, 11thEdition, 1989, Merck and Co., p. 132.
Ngo et al., 1994, The Protein Folding Problem and Tertiary Structure Prediction, pp. 492-495.
Wells, Aditivity of Mutational Effects in Proteins, 1990, Biochemistry, vol. 26, No. 37, pp. 8509-8517.
Lee, J.K., et al., “Purification of Human Interferon-β from RecombinantE. coli,” Korean Biochemical Journal, 1990, pp. 166-171, vol. 23(2).
Pepinsky, R.B., “Selective Precipitation of Proteins from Guanidine Hydrochloride-Containing Solutions with Ethanol,”Analytical Biochemistry, 1991, pp. 177-181, vol. 195.
Russell-Harde, D., et al., “The Use of Zwittergent 3-14 in the Purification of Recombinant Human Interferon-β Ser17(Betaseron),”Journal of Interferon and Cytokine Research, 1995, pp. 31-37, vol. 15(1).
Van Oss, C.J., “On the Mechanism of the Cold Ethanol Precipitation Method of Plasma Protein Fractionation,”Journal of Protein Chemistry, 1989, pp. 661-668, vol. 8(5).
Ahn, J., et al., “Investigation of Refolding Condition for Pseudomonas Fluorescens Lipase by Response Surface Methodology,”J. Biotechnol., 1997, pp. 151-160, vol. 54(3).
Bam, N., et al., “Molten Globute Intermediate of Recombinant Human Growth Hormone: Stabilization with Surfactants,”Biotechnol. Prog., 1996, pp. 801-809, vol. 12(6).
Carpenter, J., and J.H. Crowe, “The Mechanism of Cryoprotection of Proteins by Solutes,”Cryobiology, 1988, pp. 244-255, vol. 25(3).
Charman, S., et al., “Techniques for Assessing the Effects of Pharmaceutical Excipients on the Aggregation of Porcine Growth Hormone,”Pharm. Res., 1993, pp. 954-962, vol. 10(7).
Cleland, J., et al., “Polyethylene Glycol Enhanced Protein Refolding,”Biotechnology, 1992, pp. 1013-1019, vol. 10(9).
Daugherty, D., et al., “Artificial Chaperone-Assisted Refolding of Citrate Synthase,”J. Biol. Chem., 1998, pp. 33961-33971, vol. 273(51).
Dryden, D., and M.P. Weir, “Evidence for an Acid-Induced Molten-Globule State in Interleukin-2; A Fluorenscence and Circular Dichroism Study,”Bioichim. Biophys. Acta, 1991, pp. 94-100, vol. 1078(1).
Edy, V., et al., “Stabilisation of Mouse and Human Interferons by Acid pH Against Inactivation Due to Shaking and Guanidine Hydrochloride,”Proc. Soc. Exp. Biol. Med., 1974, pp. 249-253, vol. 146(1).
Edy, V., et al., “Stable and Unstable Forms of Human Fibroblast Interferon,”Infect. Immun., 1977, pp. 445-448, vol. 16(2).
Gauthier, M., and P. A. Patston, “Reactivation of C1-Inhibitor Polymers by Denaturation and Gel-Filtration Chromatography,”Anal. Biochem., 1997, pp. 228-233, vol. 248(2).
Houry, W., et al., “The Nature of the Initial Step in the Conformational Folding of Disulphide-Intact Ribonuclease A,”Nat. Struct. Biol., 1995, pp. 495-503, vol. 2(6).
Jariwalla, R., et al., “The Reactivation of Human Interferons by Guanidine Thiocyanate,”Experientia, 1980, pp. 1390-1391, vol. 36(12).
Kendrick, B., et al., “Quantitation of the Area of Overlap Between Second-Derivative Amide I Infrared Spectra to Determine the Structural Similarity of a Protein in Different States,”J. Pharm. Sci., 1996, pp. 155-158, vol. 85(2).
Muzammil, S., et al., “Molten Globule-Like State of Human Serum Albumin at Low pH,”Eur. J. Biochem., 1999, pp. 26-32, vol. 266(1).
Rozema, D., and S. H. Gellman, “Artificial Chaperone-Assisted Refolding of Denatured-Reduced Lysozyme: Modulation of the Competition Between Renaturation and Aggregation,”Biochemistry, 1996, pp. 15760-15771, vol. 35(49).
Rozema, D., and S. H. Gellman, “Artificial Chaperone-Assisted Refolding of Carbonic Anhydrase B,”J. Biol. Chem., 1996, pp. 3478-3487, vol. 271(7).
Todhunter, R., et al., “Structure of Equine Type I and Type II Collagens,”Am. J. Vet. Res., 1994, pp. 425-431, vol. 55(3).
Weir, M., et al., “Micropreparative Purification of Recombinant Human Interleukin-2,”J. Chromatogr., 1987, pp. 209-215, vol. 396.
Xie, Y. and D. B. Wetlaufer, “Control of Aggregation in Protein Refolding: The Temperature-Leap Tactic,”Protein Sci., 1996, pp. 517-523, vol. 5(3).

Affiliated with

Also associated with

Rating

Methods of protein purification and recovery does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Methods of protein purification and recovery, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods of protein purification and recovery will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4144666