Superoxide dismutase

Details Superoxide dismutase Superoxide dismutase

1990-08-27

1992-07-14

Patterson, Charles L.

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Oxidoreductase

4352402, 4353201, 536 27, 935 14, 935 22, 935 70, C12N 902, C12N 1553

Patent

active

051302454

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.
Affinity Chromatography; Principles and Methods (1979) Pharmacia Fine Chemical, pp. 92-93.
Southern, P., et al. in "Eukarydic Vinal Vectors", Cold Spring Harbor Lab (Y. Gluzman, ed.) (1982), pp. 41-45.
Suggs, et al. (1981) Biochemistry 78(11), 6613.6617.
Marklund, S. L. (1982) Proc. Natl. Acad. Sci, USA 79, 7634-7638.
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., "A 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.
Hjalmarsson et al., "Isolation and Sequence of Complementary DNA Endocing 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, Nov. 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), vol. 99, No. 5.
Hering et al., "The Primary Structure of Procine Cu-Zu 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", Nucleic Acids Res. 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", Carlsberg 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, Cytochrome C and Cytochrome C551", J. Mol. Biol., 61:409-424 (1971).
Botstein, et al., "Strategies and Applications of In Vitro Mutagenesis", 229:1193-1201, Science, (Sep. 20, 1985), No. 4719.
Fasano, et al., "Analysis of the Transforming Potential of the Human H-ras Gene by Random Mutagenesis", Proc. Natl. Acad. Sci. USA, 81:4008-4012 (Jul. 1984).
Suzuki et al. "Domain Structure of Vitronectin", J. Biol. Chem., 259:15307-15314, Nov. 24, 1984.
Calaycay et al. "Primary Structure of a DNA-- and Heparin--binding, Domain (Domain III) in Human Plasma Fibronectin 38 , J. Biol. Chem., 260:12136-12141, (1985).
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).
Fuchsman, Archives of Biochem. and 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, Superoxide Dismutases: 64.
R. Lathe, Synthetic Oligonucleotide Probes, Etc., J. Mol. Biol. 183: 1-12 (1985).
Botstein, et al., Strategies and Applications, Etc., Science, 229: 1193-1201 (Sep. 1985) (missing p. 1194).
Duplay, et al., Linker mutagenesis, Etc., Biochimie, 67: 849-851 (1985).
Milton, et al., In Vitro Mutagenesis and Overexpression, Etc., The Journ. of Biological Chem., 261: 16604-16615 (1986).
Schneider, et al., Procedure for Production of Hybrid, Etc., Proc. Natl. Aca. Sci, 78: 2169-2173 (1981).
Wang, et al., Site-Specific Mutagenesis, Etc., Science 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 Muta

Affiliated with

Also associated with

Rating

Superoxide dismutase does not yet have a rating. At this time, there are no reviews or comments for this patent.

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

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-334183