Methods and compositions for production of recombinant peptides

Details Methods and compositions for production of recombinant peptides Methods and compositions for production of recombinant peptides

2005-08-30

2005-08-30

Wax, Robert A. (Department: 1653)

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Recombinant dna technique included in method of making a...

C530S350000, C530S412000, C435S070100

Reexamination Certificate

active

06936437

ABSTRACT:
This invention provides a method for solubilizing and recovering in bioactive form, a target polypeptide or protein that has been expressed from a host organism in insoluble form. The polypeptide is isolated from the host organism by standard procedures including disrupting the host cell to produce a lysate and recovering the precipitate from the lysate. The precipitate containing the polypeptide is solubilized in a non-denaturant and detergent free non-buffered solubilization solution containing sodium hydroxide between 8 and 10 mM, mannitol between 2 and 5 mM and lactose between 1 and 2 mM. The resultant solubilization preparation contains a biologically active target polypeptide between 1 and 4 mg per ml of solubilization solution. The solubilized polypeptide obtained in this particular manner constitutes the object of the invention. The bioactive solubilized polypeptide is then transferred into an appropriate buffered solution of the desired pH and purified following conventional chromatographic procedures.

REFERENCES:
patent: 4677196 (1987-06-01), Rausch et al.
patent: 4748234 (1988-05-01), Dorin et al.
patent: 5523215 (1996-06-01), Cousens et al.
patent: 5530100 (1996-06-01), Darling et al.
patent: 5560937 (1996-10-01), Lee et al.
patent: 5834210 (1998-11-01), Liu et al.
Couche, Protein Inclusions Produced by Entomopathogenic Bacterium Xenorhadus nematophilus sussp. nematophilus, Aug. 1987, Journal of Bcteriology vol 169, No 11 pp. 5379-5287.
Moses, Marsha. Troponin I is present in human cartilage and inhibits angiogenesis. Proc. National Acad. Science USA. vol. 96. pp2645-2650. Mar. 1999.
“Recombinant-DNA-derived bovine growth hormone fromEscherichia coli”, Keith E. Langley et. al.,Eur J. Biochem. 163, pp 313-321, (1987).
“Plasminogen activator inhibitor-1 fused with erythropoietin (EPO) mimetic peptide (EMP) enhances the EPO activity of EMP”, Le-tian Kuai et.al.,J. Peptide Res., 56, 2000, pp 59-62.
“Biopharmaceutical formulation”, J. Ching Lee,Current Opinion in Biotechnology, 2000, 11, pp 81-84.
“Purification and Characterization of Human Interleukin-1 Expressed inEscherichia coli”, Shirley R. Kronheim et.al.,Bio Technology, vol. 4, Dec. 1986, pp 1078-1082.
“Expression, renaturation and purification of recombinant human interleukin 4 fromEscherichia coli”, Anita van Kimmenade et. al.,Eur. J. Biochem, pp 109-114 (1988).
Expression of a biologically active fragment of human IgE ε chain inEscherichia coli, Fu-Tong Liu et. al.,Proc. Natl. Acad. Sci. USA, vol. 81, pp 5369-5373, Sep. 1984.
“Renaturation ofEscherichia coliTryptophanase after Exposure to 8 M Urea. Evidence for the Existence of Nucleation Centers”, Jacqueline London et. al., Eur.J. Biochem. 47, 409-415 (1974).
“Inclusion Bodies from Proteins Produced at High Levels inEscherichia coli”, Joanna K. Krueger et. al.,Amer. Assoc. for the Adv. Science, 1990, pp 136-142.
“Refolding of Recombinant Proteins”, Tadahiko Kohno et. al.,Methods in Enzymology, vol 185, pp 18-195, 1990.
“E. coliexpression and characterization of a mutant troponin I with the three cysteine residues substituted”, Lan Kluwe et. al.,FEBS, vol. 323, No. 1,2, pp 83-88, May 1993.
Production of a biologically active novel goldfish growth hormone inEscherichia coli, Soheil S. Mahmoud et. al.,Comparative Biochemistry and Physiological, Part B, vol. 120, 1998, pp 657-663.
“Intermediates in the Folding Reactions of Small Proteins”, Peter S. Kim et. al.,Annu. Rev. Biochem, 1990, 59, 631-660.
“Refolding and Association of Oligomeric Protiens”, Rainer Jaenicke et. al.,Methods in Enzymology, 1986, 131, pp 218-250.
“Preparation of Biologically Active Platelet-Derived Growth Type BB from a Fusion Protein Expressed inEscherichia coli”, J. Hoppe et al ,Biochemistry, 1989, 28, 2956-2960.
“Pathways of Protein Folding”, C. Robert Matthews,Annu. Rev. Biochem. 1993, 62, 653-683.
“The Purification of eukaryotic polypeptides synthesized inEscherichia coli”, Fiona A. O. Marston,Biochem. J. (1986), 240, 1-12.
“Purification of biologically active simian virus 40 small tumor antigen”, Han Bikel et. al.,Proc. Natl. Acad. Sci. USA, vol. 80, pp 906-910, Feb. 1983.
“Recombinant Chicken and Bovine Growth Hormones Accelerate Growth in Aquacultured Juvenile Pacific SalmonOncorhynchus Kisutch”, Jacqueline, A. Gill et. al,Bio/Technology, vol 3, Jul. 1985, pp 643-646.
“Renaturation of Enzymes after Polyacrylamide Gel Electrophoresis in the Presence of Sodium Dodecyl Sulfate”, Sanford A. Lacks et. al.,The Journal of Biological Chemistry, vol. 255, No. 15, Aug. 10, 1980, pp 7467-7473.
“Cloning and expression of cDNA for salmon growth hormone inEscherichia coli”, Susumu Sekine et. al.,Proc. Natl. Acad. Sci. USA, vol. 82, Jul. 1985, pp 4306-4310.
Purification of Calf Prochymosin (Prorennin) Synthesized inEscherichia coli, Fiona A.O. Marston et. al.,Bio/Technology, Sep. 1984, pp 800-804.
“Expression and equilibrium denaturation of cardiac troponin I: stabilization of a folding intermediate during denaturation by urea”, Nihmat Morjana et al.,Biotechnol. Appl. Biochem. (1998), 28, pp 7-17.
“The Cyanogen Bromide Reaction”, Erhard Gross,Cleavage of Peptide Chains, pp 238-263.
“Gel Electrophoresis and Isoelectric Focusing of Proteins—Selected Techniques”, R.C. Allen et. al., 1984.
“In vitro folding of inclusion body proteins”, Rainer Rudolph et. al.,The FASEB Journal, Jan. 1996, vol 10, pp 49-56.
“Purification and Immunogenicity of Fusion VPI Protein of Foot and Mount Disease Virus”, Steven J. Shire et. al.,Biochemistry, 1984, 23, 6474-6480.
“Examination of calf prochymosin accumulation inEscherichia coli: disulphide linkages are a structural component of prochymosin-containing inclusion bodies”, J.M. Schoemaker et. al.,The EMBO Journal, 1985, vol. 4, No. 3, pp 775-780.
“Recovery of soluble human renin from inclusion bodies produced in recombinantEscherichia coli”, Satish K. Sharma,Journal of Biotechnology, 4 (1986) 119-124.
“Isolation and purification of protein granules fromEscherichia colicells overproducing bovine growth hormone”, Ronald G. Schoner et. al.,Bio Technology, Feb. 1985, pp 151-154.
“Size and density of protein inclusion bodies”, G. Taylor et. al.,Bio/Technology, vol 4, Jun. 1986, pp 553-557.
“Alteration of catalytic properties of chymosin by site-directed mutagenesis”, Junko Suzuki et. al.,Protein Engineering, vol. 2, No. 7, pp 563-569, 1989.
“Site-directed mutagenesis reveals functional contribution of Thr218, Lys220 and Asp304 in chymosin”, Junko Suzuki et. al.,Protein Engineering, vol. 4, No. 1, pp 69-71, 1990.
Purification of recombinant salmon growth hormone expressed inEscherichia coli, Seiji Sugimoto,Biotechnology Letters, vol. 13, No. 6, 389-394, (1991).
“Protein engineering to optimize recombinant protein purification”, Mathias Uhlen et. al.,Biochemical Society Transactions, vol 16, pp 111-115, 1988.
“Solubilization and activation of recombinant calf prochymosin fromEscherichia coli”, Fiona A. O. Marston, et al .613thMeeting, Cardiff, vol. 13, p. 1035.
“Sequencing of a cDNA encoding the human fast-twitch skeletal muscle isoform of troponin 1”, Lei Zhu et. al.Biochimica et Biophysica Acta1217 (1994) 338-340.
“Reconstitution of Lactic Dehydrogenase, Noncovalent Aggregation vs. Reactivation. 1. Physical Properties and Kinetics of Aggregation”, Gerd Zettlmeissl et. al.,Physical Properties of LDH Aggregates, vol 18, No. 25, 1979, 5567-5571.
“Increase of Solubility of Foreign Proteins inEscherichia coliby Coproduction of the Bacterial Thioredoxin”, Takashi Yasukawa:The Journal of Biological Chemistry, vol. 270, No. 43, Oct. 27, 1995, pp 25328-25331.
“Efficient and Rapid Affinity Purific

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