Chaperone protein containing an intramolecular...

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Enzymatic production of a protein or polypeptide

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S183000, C530S300000, C530S399000

Reexamination Certificate

active

06924120

ABSTRACT:
The present invention relates to a chimeric protein containing an intramolecular chaperone (IMC) like sequence linked to a target protein, preferably an insulin precursor. The present invention also relates to a process for obtaining a correctly folded insulin-precursor-contain chimeric protein, comprising, inter alia, contacting an incorrectly folded chimeric protein containing an IMC like sequence linked to an insulin precursor with at least one chaotropic auxiliary agent. The present invention further relates to an assay for screening an amino acid sequence for the ability to improve folding of an insulin precursor using a chimeric protein containing an IMC like sequence linked to an insulin precursor.

REFERENCES:
patent: 4342832 (1982-08-01), Goeddel et al.
patent: 4665160 (1987-05-01), Seeburg
patent: 4916212 (1990-04-01), Markussen et al.
patent: 5254463 (1993-10-01), de Boer et al.
patent: 5358857 (1994-10-01), Stengelin et al.
patent: 5422110 (1995-06-01), Potter et al.
patent: 5473049 (1995-12-01), Obermeier et al.
patent: 5559128 (1996-09-01), Chakravarty et al.
patent: 5719021 (1998-02-01), Inouye
patent: 6001604 (1999-12-01), Hartman et al.
patent: 2002/0164712 (2002-11-01), Gan
patent: 1341211 (2001-03-01), None
patent: 0 055 945 (1982-07-01), None
patent: 0 645 454 (1995-03-01), None
patent: WO 96/20724 (1996-07-01), None
patent: 98/23888 (1996-08-01), None
patent: WO 97/18233 (1997-05-01), None
patent: WO 02/079251 (2002-10-01), None
Moore & Kelly (May 22, 1986) “Re-routing of a secretary protein by fusion with human growth hormone sequences.” Nature 321(6068): 443-446.
Cattini & Eberhardt (Feb. 11, 1987) “Regulated expression of chimaeric genes containing the 5′-flanking regions of human growth hormone-related genes in transiently transfected rat anterior pituitary tumor cells.” Nucleic Acids Research 15(3): 1297-.
Gell et al. (Aug. 1, 1989) “Synthesis and sequence-specific proteolysis of a hybrid protein (colicin A::growth hormone releasing factor)produced inEscherichia coli.” Gene 80(1): 129-136.
Hirt et al. (Feb. 1987) “The Human Growth Hormone Gene Locus: Structure, Evolution, and Allelic Variations.” DNA 6(1): 59-70.
Liebhaber et al. (Oct. 25, 1986) “Synthesis of Growth Hormone-Prolactin Chimeric Protein and Processing Mutants by the Exchange and Deletion of Genomic Exons.” The Journal of Biological Chemistry 261(30): 14301-14306.
Bork et al . 1996, Trends in Genetics 12:425-427.
Brenner, 1999, Trends in Genetics 15:132-133.
Smith et al., 1997, Nature Biotechnology 15:1222-1223.
Doerks et al., 1998, Trends in Genetics 14:248-250.
Skolnick et al., 2000, Trends in Biotech. 18(1): 34-39.
Bork, 2000, Genome Reserch 10:398-400.
Ngo et al., 1994. The Protein Folding Problem and Tertiary Structure Prediction, pp. 492-295.
Wells, 1990, Biochemistry 29: 8509-8517.
Samuelsson et al., 1994, “Enhanced in vitro refolding of insulin-like growth factor J using a solubilizing fusion partner,”Biochemistry33(14):4207-4211 (abstract).
Klappa et al., 1997, “Interactions between protein disulphide isomerase and peptides.”European Journal of Biochemistry248(1):37-42 (abstract).
U. Shinde and M. Inouye, “Intramolecular chaperones and protein folding,”TIBS,(1993), vol. 18, pp. 442-446.
M. Inouye, “Intramolecular Chaperone: The Role of the Pro-Peptide in Protein Folding,”Enzyme,(1991), vol. 45, pp. 314-321.
M. Ikehara, et al., “Synthesis of a gene for human growth hormone and its expression inEscherichia coli,” Proc. Natl. Acad. Sci USA,(Oct. 1984), vol. 81, pp. 5956-5960.
Watson et al., Recombinant DNA—A Short Course, Scientific American Books, W.H. Freeman Co., NY, (1983), pp. 231-241.
Norman and Litwack, “Pancreatic Hormones: Insulin and Glucagon,” in Hormones, Academic Press, Inc., NY, (1987), pp 264-317.
I. Johnson, “Human Insulin from Recombinant DNA Technology,”Science, (Feb. 11, 1983), vol. 219, pp. 632-637.
D. Williams, et al., “Cytoplasmic Inclusion Bodies inEscherichia coliProducing Biosynthetic Human Insulin Proteins,”Science,(Feb. 5, 1982), vol. 215, pp. 687-689.
R. Burgess, “Protein Purification,” inProtein Engineering,Oxender, D.L., Fox, C.F., Eds.; Alan R. Liss, Inc. NY, (1987), pp. 71-82.
R.E. Chance, et al., “The Production of Human Insulin Using Recombinant DNA Technology and a New Chain Combination Procedure,” inPeptides: Synthesis-Structure-Function,Pierce Chem. Co., Rockford, Il, (1981), pp. 721-728.
B.H. Frank and R.E. Chance, “The Preparation and characterization of human insulin of recombinant DNA origin,” in Therapeutic Agents Produced by Genetic Engineering “Quo Vadis?” Symposium. (May 29-30, 1985), Sanoff Group, Toulouse-Labège, France, pp 137-148.
R E Chance, et al., “Chemical, Physical, and Biological Properties of Recombinant Human Insulin.” in J. L. GueriguianInsulins, Growth Hormone, and Recombinant DNA Technology, Raven Press, NY, (1981), pp. 71-85.
R. D. Johnson, “The Processing of Biomacromolecules: A Challenge for the Eighties,”Fluid Phase Equilib.,(1986), 29:109-123.
D. V. Goeddel, et al., “Expression inEscherichia coliof chemically synthesized genes for human insulin,”Proc. Natl. Acad. Sci. USA.(Jan. 1979), No. 1, pp. 106-110.
J. P. Burnett, “Commercial Production of Recombinant DNA-Derived Products,” inExperimental Manipulation of Gene Expression, Academic Press, NY, (1983), pp. 259-277.
J. Etienne-Decent, “Regulation of Protein Synthesis,” inGenetic Biochemistry: From Gene to Protein,Ellis Horwood Limited, Chichester, U.K., (1988), pp. 125-127.
S. M. Wheelwright,Protein Purification: Design and Scale up of Downstream Processing, Oxford University Press; NY, (1991), p. 217.
B.H. Frank and R.E. Chance, “Two Routes for Producing Human Insulin Utilizing Recombinant DNA Technology,”Munch. Med. Wschr.,(1983), vol. 125, Suppl. 1, pp. S14-S20.
E. P. Kroeff, et al, “Production Scale Purification of Biosynthetic Human Insulin by Reversed-Phase High-Performance Liquid Chromatography,”Journal of Chromalography, (1989), vol. 461, pp. 45-61.
H. V. Tottrup and S. Carlsen, “A Process for the Production of Human Proinsulin inSaccharomyces cerevisiae.” Biotechnol. Bioeng.,(1990), vol. 35, pp. 339-348.
L. R. Castellanos-Serra, et al., “Expression and folding of an interleukin-2-proinsulin fusion protein and its conversion into insulin by a single step enzymatic removal to the C-peptide and the N-terminal fused sequence,”FEBS Letters,(1996), vol. 378, pp. 171-176.
L. Villa-Komaroff, et al., “A bacterial clone synthesizing proinsulin,”Proc. Natl. Acad. Sci. USA,(Aug. 1978), vol. 75, No. 8, pp. 3727-3731.
L. Thim, et al., “Secretion and processing of insulin precursors in yeast.”Proc. Natl. Acad. Sci. USA.(Sep. 1986), vol. 83, pp. 6766-6770.
I V Diers et al., “Yeast Fermentation Processes for Insulin Production,” in Y. H. ChiuDrug Biotechnology Regulations: Scientific Basis and Practices,Marcel Dekker. Inc., NY, (1991), pp. 166-176.
M. R. Ladisch and K. L. Kohlmann, “Recombinant Human Insulin,”Biotechnol. Prog.,(1992), vol. 8, pp. 469-478.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Chaperone protein containing an intramolecular... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Chaperone protein containing an intramolecular..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Chaperone protein containing an intramolecular... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3523662

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.