Leader sequences for the production of recombinant proteins

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...

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4351721, 4351722, 4351723, 530300, 530324, 530325, 530326, 530350, 530808, C07K 708, C07K 710

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052158969

ABSTRACT:
Disclosed is a novel polypeptide useful as a leader or trailer peptide moiety in recombinant DNA protein production techniques involving fused protein methodology The polypeptide comprises an amphiphilic helix designed at the DNA level to have hydrophilic charged amino acid residues on one side of the barrel of the helix and nonpolar amino acid residues on the other side of the barrel of the helix. When DNA encoding the helix is attached to a gene encoding a protein of interest, high level expression is achieved and inclusion bodies are spontaneously formed. The inclusion bodies may be collected and purified easily by altering the ionic strength and/or pH of media used to dissolve the inclusion bodies. After purification, the fused protein is cleaved to separate the amphiphilic helix from the product.

REFERENCES:
patent: 4366246 (1982-12-01), Riggs
patent: 4425437 (1984-01-01), Riggs
patent: 4431739 (1984-02-01), Riggs
patent: 4543329 (1985-09-01), Daum
patent: 4563424 (1986-01-01), Riggs
patent: 4743679 (1988-05-01), Cohen et al.
patent: 4751180 (1988-06-01), Cousens et al.
patent: 5004686 (1991-04-01), Cohen et al.
patent: 5013653 (1991-05-01), Huston et al.
Marston, F. A, Review Article, Biochem. J., 240: 1-12, 1986.
Kaiser, E. T, et al., "Amphiphilic Secondary Structure: Design of Peptide Hormones", Science, 223, pp. 249-255, 1984.
Chou, P. Y, et al., "Empirical Predictions of Protein Conformations", Ann. Rev. Biochem., 47:251-76, 1978.
Sung, W. L., et al., "Short Synthetic Oligodeoxyribonucleonide leader sequences enhance accumulation of human proinsulin", PNAS, USA., 83:561-5, 1986.
Lau, S. H., et al., "Surface properties of an amphiphilic peptide hormone and its analog: corticotropin-releasing factor and sauvagine", PNAS, U.S.A., 80, pp. 7070-7074, 1983.
Sassenfeld and Brewer, "A polypeptide fusion designed for the purification of recombinant proteins". Biotech. (1984), 76-81.
Nagai and Thogersen, "Generation of B-globin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coli." Nature (1984) 309:810-812.
Germino and Bastia, "Rapid purification of a cloned gene product by genetic fusion and site-specific proteolysis." Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4692-4696.
Nisonoff, Introduction to Molecular Immunology Sinauer Associates, (1982), pp. 22-23.
Brewer and Sassenfeld, "The purification of recombinant proteins using C-terminal polyargineni fusions." Trends in Biotech. (1985) 3:119-122.
Uhlen et al, "Gene fusion vectors based on the gene for staphylococcal protein A." Gene. (1983) 223:369-378.
Germino et al, "Use of gene fusions and protein-protein interaction in the isolation of a biologically active regulatory protein: The replication initiator protein of plasmid R6K." Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6848-6852.
Epand, (1983) The amphipatic helix: its possible role in the interaction of glucagen and other peptide hormones with membrane receptor sites. Trends in Biochem. Sci 9:67-69.
Blanc et al., (1983) Examination of the requirements for an amphiphilic hilical structure in B-endorphin through the design, synthesis and study of model peptides. J. Biol. Chem. 258:8277-8284.
Taylor et al., (1983) Characterization of an amphiphilic helical structure in B-endorphin through the design, synthesis and study of model peptides, J. Biol. Chem. 258:4464-4471.
Shoemaker et al., (1985) Nature of the charged-group effect on the stability of the C-peptide helix. Proc. Natl. Acad. Sci. U.S.A. 82:2349-2353.
Giniger, E., et al., Nature, 330:670-672, Dec. 1987.
Degrado et al., J. American Chemical Soc., vol. 103, No. 3, 1981, pp. 679-681.
Ho et al., J. American Chemical Soc., vol. 109, No. 22, 1987 pp. 6751-6758.
Lau et al., J. Biological Chemistry vol. 259, No. 21, pp. 13253-13261; 1984.
Taylor et al., J. of Biological Chemistry, vol. 258, pp. 4464-4471, 1983.
Fukushima et al., J. Am. Chem. Soc. 101:3703 (1979).
Moe et al., Amer. Chem. Soc. 24:1972 (1985).
Musso et al., Biochem. Biophys. Res. Comm. 119:713 (1984).
Yokoyama et al., J. Biol. Chem. 225:7333 (1980).

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