Method of purifying TFPI and TFPI analogs

Details Method of purifying TFPI and TFPI analogs Method of purifying TFPI and TFPI analogs

2004-01-08

2010-12-14

Carlson, Karen Cochrane (Department: 1656)

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Peptide containing doai

C530S350000

Reexamination Certificate

active

07851433

ABSTRACT:
Highly purified preparations of TFPI or TFPI analogs can be prepared using a method that generally involves the following steps: (1) expression of TFPI or TFPI analog inE. coli, (2) isolation of refractile bodies, (3) dissolution of the refractile bodies and refolding of the expressed TFPI or TFPI analog, (4) SP-Sepharose fast flow (FF) chromatography, (5) a first concentration and diafiltration step, (6) Q-Sepharose high (HP) performance chromatography, (7) butyl hydrophobic interaction chromatography (HIC), (8) SP-Sepharose HP chromatography, and (9) a second concentration/diafiltration step. Less than about 12% of the TFPI or TFPI analog molecules in such preparations are modified TFPI or TFPI analog species (i.e., oxidized, carbamylated, acetylated, deamidated, aggregated, or misfolded species).

REFERENCES:
patent: 4637834 (1987-01-01), Thurow
patent: 4966852 (1990-10-01), Wun et al.
patent: 5051497 (1991-09-01), Fanning et al.
patent: 5212091 (1993-05-01), Diaz-Collier et al.
patent: 5276015 (1994-01-01), Khouri et al.
patent: 5358708 (1994-10-01), Patel
patent: 5466783 (1995-11-01), Wun et al.
patent: 5503827 (1996-04-01), Woog et al.
patent: 5563123 (1996-10-01), Innis et al.
patent: 5589359 (1996-12-01), Innis et al.
patent: 5824644 (1998-10-01), Abendschein
patent: 5885781 (1999-03-01), Johnson et al.
patent: 5902582 (1999-05-01), Hung
patent: 6063764 (2000-05-01), Creasey et al.
patent: 6103500 (2000-08-01), Innis et al.
patent: 6242414 (2001-06-01), Johnson
patent: 6319896 (2001-11-01), Arve et al.
patent: 6323326 (2001-11-01), Arve et al.
patent: 6525102 (2003-02-01), Chen et al.
patent: 2002/0137884 (2002-09-01), Arve et al.
patent: 0 473 564 (1992-03-01), None
patent: 0 559 632 (1993-09-01), None
patent: 0 559 632 (1993-09-01), None
patent: 0 414 374 (1997-10-01), None
patent: 0 755 438 (2001-02-01), None
patent: WO 93/18150 (1993-09-01), None
patent: WO 93/24143 (1993-12-01), None
patent: WO 93/25230 (1993-12-01), None
patent: WO 96/01272 (1996-01-01), None
patent: WO 96/01273 (1996-01-01), None
patent: WO 96/01649 (1996-01-01), None
patent: WO 96/04378 (1996-02-01), None
patent: WO 96/40224 (1996-12-01), None
patent: WO 97/09063 (1997-03-01), None
patent: WO 99/57280 (1999-11-01), None
patent: WO 01/64922 (2001-09-01), None
patent: WO 03/032904 (2003-04-01), None
patent: 2005/019265 (2005-03-01), None
Hwang et al., “Co-Expression of glutathione S-transferase with methionine aminopeptidase: A system of producing enriched N-terminal processed proteins inEscherichia coli”, Biochemical Journal, vol. 338, No. 2, Mar. 1, 1999, pp. 335-342.
Ben-Bassat et al., “Processing of the initiation methionine from proteins: properties of theEscherichia colimethionine aminopeptidase and its gene structure”, Journal of Bacteriology, vol. 169, No. 2, Feb. 1987, pp. 751-757.
Rainer Rudolph, “Successful Protein Folding on an Industrial Scale”, Protein Engineering: Principles and Practice, Chapter 10, pp. 283-298 (1996).
Dabora et al., “Effect of Polyanions on the Refolding of Human Acidic Fibroblast Growth Factor”, The Journal of Biological Chemistry, vol. 266, No. 35, pp. 23637-23640 (1991).
Bernhard Fisher et al., “Isolation, Renaturation, and Formation of Disulfide Bonds of Eukaryotic Proteins Expressed inEscherichia colias Inclusion Bodies”,Biotechnology and Bioengineering, vol. 41, pp. 3-13 (1993).
J. Harenberg, et al., Tissue Factor Pathway Inhibitor: Proposed Heparin Recognition Region,Blood Coagulation and Fibrinolysis, vol. 6, Supp. No. 1, pp. S50-S56 (1995).
Mark E. Gustafson et al., “Renaturation and Purification of Human Tissue Factor Pathway Inhibitor Expressed in RecombinantE. coli, Protein Expression and Purification”, vol. 5, pp. 233-241 (1994).
Curless et al., “Phosphate Glass as a Phosphate Source in High Cell DensityEscherichia coliFermentations”,Biotechnology Progress, vol. 12, pp. 22-25 (1996) XP002238061.
Malaoui et al., “Influence of Glucose on Glycerol Metabolism by Wild-Type and Mutant Strains ofColostridium butyricumE5 grown in Chemostat Culture”,Applied Microbiology and Biotechnology, vol. 55, Dec. 2000, pp. 226-233, XP002237996.
Vagabov et al., “Dependence of Inorganic Polyphosphate Chain Length on the Orthophosphate Content in the Culture Medium of the YeastSaccharomyces Cerevisiae”, Biochemistry(Moscow), vol. 65, 2000, pp. 349-354, XP002237997.
Albertson et al., “Growth and Survival ofHelicobacter pyloriin Defined Medium and Susceptibility to Brij 78”,Journal of Clinical Microbiology, vol. 36, 1998, pp. 1232-1235, XP002238062.
Bauer et al., “Improved Expression of Human Interleukin-2 in High-Cell-Density-Density Fermentor Cultures ofEscherichia coliK-12 by a Phosphotransacetylase Mutant”, 1990,Appl. Environ. Microbiol.I, 56: 1296-1302.
Bonsignore et al., “Development of a Chemically Defined Medium for Bacterial Biotin Production”, 1989,Abstr. Pap. Am. Chem. Soc.198 Meet, MBTD 199.
Box & Wilson, “On the Experimental Attainment of Optimum Conditions”, 1951,J. Roy. Statist. Soc., B13: 1-45.
Chalmers et al., “Effects of Temperature onEscherichia coliOverproducing β-Lactamase or Human Epidermal Growth Factor”, 1990,Appl. Environ. Microbiol., 56: 104-111.
Evans, D.J. et al., “Identification of Four New Prokaryotic Bacterioferritins, fromHelicobacter pylori, Anabaena variabilis, Bacillus subtilisandTreponema pallidum, byAnalysis of Gene Sequence”, 1995, Gene, 153: 123-127.
De Vuyst, L., “Nutritional Factors Affecting Nisin Production byLactococcus lactusSubsp.Lactis NIZO 22186in a Synthetic Medium”, 1995,J. Appl. Bacteriol., 78: 28-33.
Galindo et al., “Maximizing the Expression of Recombinant Proteins inEscherichia coliby Manipulation of Culture Conditions”, 1990,J. Ferm. Bioeng., 69: 159-165.
Konstantinov et al., “Physiologically Motivated Strategies for Control of the Fed-Batch Cultivation of RecombinantEscherichia colifor Phenylalanine Production”, 1991,J. Ferm. Bioeng., 71: 350-355.
Kopetzki et al., “Control of Formation of Active Soluble or Inactive Insoluble Baker's Yeast α-Glucosidase Pl inEscherichia coliby Induction and Growth Conditions”, 1989,Mol. Gen. Genet., 216: 149-155.
Lee & Lee, “Enhanced Production of Poly(3-hydroxybutyrate) by Filamentation-Suppressed RecombinantEscherichia coliin a Defined Medium”, 1996,Journal of Environmental Polymer Degradation, 4(2): 131-134.
Luli & Strohl., “Comparison of Growth, Acetate Production, and Acetate Inhibition ofEscherichia coliStrains in Batch and Fed-Batch Fermentations”, 1990,Appl. Environ. Microbiol., 56: 640-645.
MacDonald & Neway, “Effects of Medium Quality on the Expression of Human Interleukin-2 at High Cell Density in Fermentor Cultures ofEscherichia coliK-12”, 1990,Appl. Environ. Microbiol., 56: 640-645.
Manetti, R. et al., “Helicobacter pyloriCytotoxin: Importance of Native Conformation for Induction of Neutralizing Antibodies”, 1995,Infect. Immun., 63: 4476-4480.
Okita et al., “Effect of Induction Temperature on the Production of Malaria Antigens in RecombinantE. coli”, 1989,Biotechnol. Bioeng., 34: 854-862.
Park & Ryu, “Effect of Operating Parameters on Specific Production Rate of a Cloned-Gene Product and Performance of Recombinant Fermentation Process” 1990,Biotechnol. Bioeng., 35: 287-295.
Rappuoli et al., “Development of a Vaccine AgainstHelicobacter Pylori: A Short Overview”, 1993,European Journal of Gastroenterology and Hepatology of Helicobacter Pylori Infection, Proceedings of an Interdisciplinary Meeting (Geneva, Jun. 18-19, 1993) J.J. Misiewicz, Ed. (CS Current Science) pp. S76-S78.
Rappuoli, R., “Toxin Inactivation and antigen Stabilization: Two Different Uses of Formaldehyde”, 1994,Vaccine, 12(7): 579-581.
Rinas et al., “Glucose as a Ssubstrate in Recombinant Strain F

Affiliated with

Also associated with

Rating

Method of purifying TFPI and TFPI analogs does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Method of purifying TFPI and TFPI analogs, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Method of purifying TFPI and TFPI analogs will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4217169