Superoxide dismutase

Details Superoxide dismutase Superoxide dismutase

1995-05-19

1998-08-04

Patterson, Jr., Charles L.

Drug, bio-affecting and body treating compositions

Enzyme or coenzyme containing

Oxidoreductases

435189, A61K 3844

Patent

active

057889619

ABSTRACT:
A superoxide dismutase originally found in extracellular body fluids and therefore termed extracellular superoxide dismutase (EC-SOD) is prepared by growing a cell line, preferably of mammalian origin, producing EC-SOD and recovering the EC-SOD secreted from the cells or by inserting a DNA sequence encoding EC-SOD into a suitable vector, introducing the recombinant vector into a host cell, growing the cell and recovering the EC-SOD produced.
EC-SOD may be used for the prophylaxis or treatment of diseases or disorders associated with the presence or formation of superoxide radicals.

REFERENCES:
patent: 4530901 (1985-07-01), Weissmann
patent: 4738927 (1988-04-01), Taniguchi et al.
Marklund, CA 101:36464x; Mammalian Superoxide Dismutase (1984).
Fujisawa, CA 103:176901d; Superoxide Dismutase Production Using Monoclonal Antibodies (1985).
Affinity Chromotography, Principles and Methods (1979), Pharmaciz Fine Chemicals, pp. 92-93.
Southern, et al. in "Eukaryotic Viral Vectors", Cold Spring Harbor Lab (Y. Gluzman, ed.) (1982), pp. 41-45.
Suggs, et al., "Use of synthetic oligonucleotides as hybridization probes: Isolation of cloned cDNA sequences for human Beta2-microglubulin", Biochemistry 78:11:6613-6614, (Nov. 1981).
Marklund, S.L., "HUman copper-containing superoxide dismutase of high molecular weight", Proc. Natl. Acad. Sci. USA, 79:7634-7638, (Dec. 1982).
Kortt, et al., Eur. J. Biochem., 175: 141-49 (1988).
Zimmerman, Biol. Chem. Hoppe-Seyler, 369: 93-96 (Feb. 1988).
Chen, et al., Biochem. J., 203: 33-43 (1982).
Ozols, et al., The Journ. of Biological Chem., 244: 6617-6618 (Dec. 25, 1969).
Gibson, et al., The Journal of Biological Chem., 263: 4182-85 (Mar. 1988).
Fuchsman, Archives of Biochem. adn Biophysics, 243: 454-60 (Dec. 1985).
Mazrimas, et al., A Corrected Primary Sequence for Bull Protamine Biochimica et Biophysica Acta 872: 11-15 (1986).
Hu, et al., Cloning and Characterization of the Gene, Etc., Biochemistry 25: 7834-7839 (1986).
Panneerselvan, et al., Bovine Parathymosin: Amino Acid Sequence, Etc., Biochem & Biophys. Res. Comm., 155: 539-545 (Sep. 1988).
Mitchel, et al., The Complete Amino Acid, Etc., The Journal of Biological Chem., 245: 3485-3492 (1970).
Knecht, et al., Sequence Determination of Eglin, Etc., Analytical Biochemistry, 130: 65-71 (1983).
Fridovich, (1974) Adv. Enz. Rel Areas, p. 64.
R. Lathe, Synthetic Oligonucleotide Probes, ETc., J. Mol. Biol. 183: 1-12 (1985).
Schneider, et al., Procedure for Production of Hybrid, Etc., Proc. Natl. Aca. Sci, 78: 2169-2173 (1981).
Wang, et al., Site-Specific Mutagenesis, Etc., 1431-1433 (Jun. 1984).
Fersht, et al., Fine Structure-Activity Analysis, Etc., Bio-Chemistry, 24: 5858-5861 (1985).
Carter, et al., The Use of Double Mutants, Etc., Cell., 38: 835-40 (Oct. 1984).
Parge, et al., Crystallographic Chracterization, ETc., The Journal of Biol. Chem., 261: 16215-18 (1986).
Beyer, et al., Examination of the Role of Arginine, Etc., 262: 11182-87 (1987).
Creighton, Structure and Molecular Princ., Proteins, 37-42, 45-47, 110-112, 128, 129, 235, 259, 352-366 (1983).
Schulz, et al., Principles of Protein Structure, 2, 3, 10-12, 14-16, 168-174 (1979).
Shively, et al., Anal. Biochem., 120: 312-322 (1982).
Marklund, Holme and Hellner, Clinica Chimica Acta 126:41-51 (1982).
Marklund, Biochem. J., 220:269-72 (1984).
Marklund, J. Clin. Invest., 74:1398-1403 (1984).
Marklund, Biochem J., 222:649-55 (1984).
Duplay et al., "Linker Mutagenesis in the GeneEncoding The Periplasmic Maltose-Binding Protein of E.Coli.", Biochimie, 1985, 67, 849-851.
Wells, et al., "Cassette Mutagenesis: An Efficient Method for Generation of Multiple Mutations at Defined Sites", Gene, 34 (1985) 315-323.
Milton et al., "In Vitro Mutagenesis and Overexpression of the Escherichia Coli trpA Gene and the Partial Characterization of the Resultant Tryptophan Synthase Mutant Alpha-Subunits", J. Bio. Chem., 261 (1986) 16604-16615.
Matteucci et al., "Integrated Random Mutagenesis: The Use of Ambiguously Synthesized Oligonucleotides to Mutagenize Sequences Immediately 5' of an ATG Initiation Codon", Nuc. Acids. Res., vol. 11, No. 10, 1983, 3113-3121.
Myers, et al., "General Method for Saturation Mutagenesis of Cloned DNA Fragments", Science, vol. 229, 242-247 (1985).
Abarzua et al., "Enzymatic Techniques for the Isolation of Random Single-Base Substitutions in vitro at High Frequency", Proc. Natl. Acad. Sci. USA, 81, 2030-2034, Apr. 1984.
Hjalmarssson et al., "Isolation and Sequence of Complementary DNA Encoding Human Extracellular Superoxide Dismutase", Proc. Natl. Acad. Sci. USA, 84: 6340-6344, Sep. 1987.
Adachi et al., "Interactions Between Human Extracellular Superoxide Dismutase C and Sulfated Polysaccharides", J. Bio. Chem., 264:8537-8541, 1989, No. 15.
Borders et al., "Identification of ARG-143 As the Essential Arginyl Residue in Yeast Cu, Zn Superoxide Dismutase by Use of a Chromophoric Arginine Reagent", Bio. and Biop. Res. Comm., 96:1071-1078, No. 3, 1980.
Malinowski et al., "Chemical Modification of Arginine at the Active Site of the Bovine Erythrocyte Superoxide Dismutase", Biochemistry, 18:5909-5917, No. 26, 1979.
Steffens, et al., "The Primary Structure of Cu-Zn Superoxide Dismutase from Photobacterium Biognathi: Evidence for a Separate Evolution of CuZn Superoxide Dismutase in Bacteria", Hoppe-Seylers Z. Phy. Chem. 364:675-90(1983).
Bannister et al., "The Presence of a Copper/Zinc Superoxide Dismutase in the Bacterium Photobacterium Leiognathi: A Likely Case of Gene Transfer From Eukaryotes to Prokaryotes", Proc. Nat. Acad. Sci., 82:149-152, Jan. 1985.
Rocha, et al., "The Amino Acid Sequence of Copper/Zinc Superoxide Dismutase from Swordfish Liver -Comparison f Copper/Zinc Superoxide Dismutase Sequences", Eur. J. Biochem., 145:477-484 (1984).
Lee et al., "Superoxide Dismutase: An Evolutionary Puzzle", Proc. Natl. Acad. Sci. USA, 82:824-828, 1985.
Steinman, "The Amino Acid Sequence of Copper-Zinc Superoxide Dismutase from Bakers' Yeast", J. Biol. Chem., 255, No. 14, 6758-6765 (1980).
Kitagawa, et al., "Amino Acid Sequence of Copper, Zinc-Superoxide Dismutase from Spinach Leaves", J. Biochem., 99:1289-1298 (1986), vol. 99, No. 5.
Hering et al., "The Primary Structure of Procine Cu-Zn Superoxide Dismutase Evidence for Allotypes of Superoxide Dismutase in Pigs", Bio. Chem. Hoppe-Seyler, 366:435-445 (Apr. 1985).
Lerch, et al., "Amino Acid Sequence of Copper-Zinc Superoxide Dismutase from Horse Liver", J. Bio. Chem., 256, No. 22, 11545-11551 (1981).
Steinman, et al., "Bovine Erythrocyte Superoxide Dismutase", J. Biol. Chem. 249, No. 22, 7326-7338 (1974).
Sherman, et al., "Nucleotide Sequence and Expression of Human Chromosome 21-encoded Superoxide Dismutase mRNA", Proc. Natl. Acad. Sci., USA, 80: 5465-5469 (Sep. 1983).
Hallewell, et al., "Human Cu/Zn Superoxide Dismutase cDNA:Isolation of Clones Synthesizing High Levels of Active or Inactive Enzyme from an Expression Library", 13, No. 6, 2017-2034 (1985).
Tainer, et al., "Determination and Analysis of the 2 A Structure of Copper, Zinc Superoxide Dismutase", J. Mol. Biol. (1982) 160, 181-217.
Bermingham-McDonogh et al., "Reduced Anion-Binding Affinity of Cu, Zn Superoxide Dismutases Chemically Modified at Arginine", 108:1376-1382 No. 4 (1982), Biochem. Biophys. Res. Commun.
Borders, Jr. et al., "Essential Arginyl Residues in Cu,Zn Superoxide Dismutase from Saccharomyces Cerevisiae", Carbohydr. Res. Commun., vol. 45, 185-194 (1980).
Getzoff et al., "Electrostatic Recognition Between Superoxide and Copper, Zinc Superoxide Dismutase", Nature, 306:287-290 (Nov. 1983).
Tainer et al., "Structure and Mechanism of Copper, Zinc Superoxide Dismutase", Nature, 306:284-286 (Nov. 1983).
Amuro, et al. "Replacement by Site-directed Mutagenesis Indicates a Role for Histidine 170 in the Glutamine Amide Transfer Function of Anthranilate Synthase", J. Biol. Chem., 260:14844-14849, No. 27 (1985).
Borders, et al., "Essentiality of the Active-Site Arginine Residue for the Normal Catalytic Activity of Cu, Zn Superoxide Dismutase", Biochem., J. 230:771-776 (1985).
McLachlan, "Tests for Comparing Related Amino-Acid Sequences, Cytoch

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