Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Hormones – e.g. – prolactin – thymosin – growth factors – etc.
Patent
1993-08-20
1997-09-02
Ulm, John
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Hormones, e.g., prolactin, thymosin, growth factors, etc.
530418, 530420, 530422, 530424, 435 694, 4351723, 4352523, 4353201, C07K 14475, C12N 1518
Patent
active
056633041
ABSTRACT:
A composition is provided comprising about 0.1 to 15 mg/mL of a polypeptide in a buffer having a pH of about 7-12 comprising about 5-40% (v/v) of an alcoholic or polar aprotic solvent, about 0.2 to 3M of an alkaline earth, alkali metal, or ammonium salt, about 0.1 to 9M of a chaotropic agent, and about 0.01 to 15 .mu.M of a copper or manganese salt. The buffer is suitably used in a method for refolding improperly folded polypeptides.
REFERENCES:
patent: 4511502 (1985-04-01), Builder et al.
patent: 4511503 (1985-04-01), Olson et al.
patent: 4512922 (1985-04-01), Jones et al.
patent: 4518256 (1985-05-01), Schwartz
patent: 4518526 (1985-05-01), Olson
patent: 4565785 (1986-01-01), Gilbert et al.
patent: 4572798 (1986-02-01), Koths et al.
patent: 4620948 (1986-11-01), Builder
patent: 4652630 (1987-03-01), Bentle et al.
patent: 4673641 (1987-06-01), George et al.
patent: 4705848 (1987-11-01), Yang et al.
patent: 4710473 (1987-12-01), Morris
patent: 4738921 (1988-04-01), Bellagaje et al.
patent: 4795706 (1989-01-01), Hsiung et al.
patent: 4923967 (1990-05-01), Bobbitt et al.
patent: 4985544 (1991-01-01), Yokoo et al.
patent: 5019500 (1991-05-01), Ieda et al.
patent: 5028531 (1991-07-01), Ueda et al.
patent: 5158875 (1992-10-01), Miller et al.
patent: 5191063 (1993-03-01), Inouye et al.
patent: 5288931 (1994-02-01), Chang et al.
Callard & Gearing (1994). The Cytokine Facts Book. Academic Press, Harcourt Brace & Co. Publishers pp. 2-3.
Marston (1986). Biochemical Journal, vol. 240, pp. 1-12.
Brems et al., "Equilibrium Denaturation of Pituitary-and Recombinant-Derived Bovine Growth Hormone", pp. 7662-7668, Biochemistry, vol. 24, No. 26, 1985.
Schein et al., "Formation of Soluble Recombinant Proteins in Escherichia coli is Favored By Lower Growth Temperatures", pp. 291-294, Biotechnology, vol. 6, Mar. 1988.
Mizukami et al., "Production of Active Human Interferon-B in E. coli I, Preperential Production By Lower Culture Temperature", pp. 605-610, Biotechnology Letters, vol. 8 No. 9, 1986.
Mitraki et al., "Protein Folding Intermediates and Inclusion Body Formation", pp. 690-697, Biotechnology, vol. 7, 1989.
Marston et al., "[20] Solubilization of Protein Aggregates", pp. 264-276, Biochem. J. 240, 1 (1986).
Wetzel, "Protein Aggregation in Vivo-Bacterial Inclusions Bodies and Mammalian Amyloid", pp. 43-89, Stability of Pharmaceeuticals, Part B:IN Vivo Pathways of Degradation and Strategies for Ptotein Stabilization, New York, 1992.
Raschdorf et al., "Location of Disulphide Bonds in Human Insulin-Like Growth Factors (IGFs) Synthesized by Recombinant DNA Technolgy", pp. 3-8, Biomedical and Environmental Mass Spectormetry, vol. 16, 1988.
Morris et al., "Protein folding/refolding analysis by mass spectrometry-Scrambling of disuphide bridges in Insulin", pp. 803-806, Biochem. J. (1990) 268.
Toren et al., "Determination of Interchain Crosslinkages in insulin B-Chain Dimers by Fast Atom Bombardment Mass Spectremetry", pp. 287-299, Analytical Biochemistry 169, (1988).
Green et al., "Cheddar cheesemaking with recobinant calf chymosin synthesized in Escherichia coli", pp. 281-286, Journal of Dairy Research, (1985).
Frank et al., "The Production of Human Proinsulin and Its Transformationto Human Insulin and C-Peptide", pp. 729-738 Rich and Gross, (1981).
Cleland et al., "Refolding an Deggregation of Bovine Carbonic Anhydrase B: Quasi-Elastic Light Scattering Analysis", pp. 11072-11078, Biochemistry, 29, 1990.
Halenbeck et al., "Renaturation and Purification of Biologically Active Recombinant Human Macrophage Colony-Stimulating Factor Expressed in E. Coli", pp. 710-715, Biotechnology, vol. 7, Jul. 1989.
Tsuji et al., "Characterization of Disulfide Bonds in Recombinant Proteins: Reduced Human Interleukin 2 in inclusion Bodies and Its Oxidative Refolding", pp. 3129-3134, Biochemistry, 26, 1987.
George et al., "High-Level Expression in Escherichia coli of Biologically Active Bovine Growth Hormone", pp. 273-281, Mary Ann Liebert, Inc. Publishers, 1985.
Gill et al., "Recombinant Chicken and Bovine Growth Hormones Accelerate Growth in Aquacultured Juvenile Pacific Salmon Oncorhynchus Kisutch", pp. 643-646, Biotechnology, vol. 3, 1985.
Sekine et al., "Cloning and expression of cDNA for salmon growth hormone in Escherichia coli", pp. 4306-4310, Proc. Natl. Acad. Sci. USA, vol. 82, 1985.
Winkler et al., "Purification and Characterization of Recombinant Urokinase from Escherichia coli", pp. 990-1000., Biotechnology, vol. 3, Nov. 1985.
Kohnert et al., "Production of a Recombinant Human Tissue Plasminogen Activator Variant (BM 06.022) from Escherichia coli Using a Novel Renaturation Technology", p. 44, Posters I, 1990.
Marston, "The purification of eukaryotic polypeptides sysnthesized in Escherichia coli", pp. 1-12, Biochem. J. 240,(1986).
Boss et al., "Assembly of functional antibodies from immunoglobulin heavy and Light chains synthesized in E. coli", pp. 3791-3806, Nucleic Acids Research, vol. 12, NO. 9, 1984.
Cabilly et al., "Generation of antibody activity from immunoglobulin polypeptide chains produces in Escherichia coli", pp. 3273-3277, Proc. Natl. Acad. Sci, USA, vol. 81. Jun. 1984.
Marston et al., "Purification of Calf Prochymosin (Proreennin) Synthesized in Echerichia coli ", pp. 800-804, Biotechnology, Sep., 1994.
Hoppe et al., "Preparation of Biologically Active Platelet-Derived Growth Factor Type BB from a Fusion Protein Expressed in Escherichia coli", pp. 2956-2960, Biochemistry, 28, 1989.
Bowden et al., "Structure and Morphology of Protein Inclusion Bodies in Escherichia coli", pp. 725-730, Biotechnology, vol. 9, Aug. 1991.
Wetzel et al., "Mutations in Human Interferon Gamma Affecting Inclusion Body Formation Identified By A General Immunochemical Screen", pp. 731-737, Biotechnology, vol. 9, 1991.
Hejnaes et al., "Development of an optimized refolding process for recombinant Ala-Glu-IGF-1", pp. 797-806, Protein Engineering, vol. 5, 1992.
Obukowicz et al., "Secretion and Export of IGF-1 in Escherichia coli strain JM101", pp. 19-25, Mol Gert Genet vol. 215 1988.
Wong et al., "Expression of secreted insulin-Like growth factor-1 in Escherichia coli", pp. 193-203), Gene, 68 (1988).
Saito et al., "Direct Expression of a Synthetic Somatomedin C Gene in Escherichia coli" by Us eof a Two-Cistron System", pp. 1281-1288, J. Biochem. 101, 1987.
Schulz et al., "Increased Expression in Escherichia coli of a Synthetic Gene Encoding Human Somatiomedin C after Gene Duplication and Fusion", pp. 5385-5392, Journal of Bacteriology, Dec. 1987.
Saito et al., "Production and Isolation of Recombinant Somatomedin C", pp. 123-134, J. Biochom. 101, 1987.
Niwa et al., "Chemical Synthesis, CLoning, and Expression of Genes for Human Somatomedin C (Insulin-Like Growth Factor I) and .sup.59 Val-Somatomedin C", pp. 31-52, Annals New York Academy of Sciences, 1986.
Hober et al., "Disulfide Exchange Folding of Insulin-Like Growth Factor 1", pp. 1749-1756, Biochemistry, 31, 1992.
Snyder, "Free Energy Relationships for Thiol-Disulfide interchange Reactions between Charged Molecules in 50% Methanol", pp. 7468-7472, The Jounral of Chemistry, vol. 12, 1984.
Funakoshi et al., "Isolation of a tumor-derived 186-residue peptide amide related to a human chromogranin A and its in vitro conversion to human pancreastatin-48", pp. 512-514, Recent bioactive Peptides and Biology, 1989.
Lustig et al., "The thermal denaturation of ribonuctease A in aqueous-methanol solvents", pp. 205-210, Biochimica et Biophysica Acta, (1992).
Bryant et al., "Detection of an Equilibrium intermediate in the Folding of a Monomeric Insulin Analog", pp. 5692-5698, Biochemistry, vol. 31, No. 25 (1992).
Hua et al., "Two-dimensional NMR studies of Des-(B26-B30)-insulin: sequence-specific resonance assignments and effects of solvent composition", pp. 101-110, Biochimica et Biophysica Acta, 1078 (1991).
Brems et al., "Equilibrium Denaturation of Insulin and Proinsulin", Biochemistry, vol. 29, (1990).
Jackson et al., "Hatogenated alcohols as solvents for proteins: FTIR spectroscopic studies", pp. 139-143, Biochimica et Biophysica Acta. 1118. )1992.
Shibata et al., "Biphasic Eff
Builder Stuart
Hart Roger
Lester Philip
Reifsnyder David
Dreger Walter H.
Genentech Inc.
Mertz Prema
Ulm John
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