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Original Article

Artificial Cell Containing Superoxide Dismutase - Selection of Folding Aids for Stabilisation of Sod

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Pages 341-358 | Published online: 04 Aug 2009

References

  • Chang T MS. Semipermeable aqueous microcapsules(“artificial cell”), Trans. Am. Soc. Artif. Intern. Organs 1966; 12: 13–19
  • Chang T MS. Artificial cells. Monograph. Charcls C Thomas, Springfield, Ill 1972
  • Zhao X B, Qian H. Studies and application of artificial cell containing superoxide dismutase (AC-SOD) in cosmetics, China Surfactant. Detergent & Cosmetics 1995; 5: 6–10
  • Cleland J L, Wang D IC. Cosolvent assisted protein refolding. Biotechnology 1990; 8: 1274–1278
  • Schaffer S W, Ahmed A, Wetlaufer DB. Salt effects in the glutathione-facilitated reactivation of reduced bovine pancreatic ribonuclease. J Biol. Chem. 1975; 250: 8483–8486
  • Valax P, Georgiou G. Protein Refolding, G Georgious, E DeBemardez Clark. American Chemical Society, Washington DC 1991; 97–109
  • Tandon S, Horwitz PM. Detergent-assisted refolding of guanidinium chloride-denatured rhodanese: The effects of the concentration and type of detergent. J. Biol. Chem. 1987; 262: 4486–4491
  • McCord J M, Fridovich I. Superoxide Dismutase. An enzymatic function for prythrocuprein (hemocuprein). J Biol Chem. 1969; 244: 6049–6055
  • McCord JM. Oxygen-derived free radical in post ischemic tissue injury. New Engl. J. Med. 1985; 312: 159–163
  • Starkebaum G. Review of rheumatoid arthritis, Recent developments. Autoimmune Dis. 1993; 13: 273–289
  • Petkau A. Role of superoxide dismutase in modification of radiation injury. Br. J Cancer 1987; 55: 87–95
  • Blebea J, Kerr J C, Hobson R W, Padberg FT. The effects of oxygen free radical scavengers on skeletal muscle ischemia and reperfusion injury. Current surgery September-October, 1987; 396–398
  • D'Agnillo F, Chang T MS. Cross-linked hemoglobin-superoxide dismutase-catalase scavenges oxygen-derived free radicals and prevents methemoglobin formation and iron release, Biomaterials, Artificial Cells and immobilization Biotechnology. An International Journal 1993; 21: 609–622
  • Lin C W, Yang J H, Su LC. The extraction and properties of superoxide dismutase from porcine blood. Meat Science 1997; 46(3)303–312
  • Jungbauer A, Schoenhofer W, Pettauer D, Gruber G, Unterluggauer F, Uhi K, Wenisch E, Steindl F. Large scale purification of human erythrocyte Cu/Zn superoxide dismutase. Biosciences 1989; 8: 21–26
  • Kramer W, Doblhoff-Dier O, Lettner H P, Pettauer D, Taferner N, Bayer K, Katinger H. Development of a control strategy for production of recombinant proteins. European Congress on Biotechnology, Copenhagen, Munksgaard 1990; 345
  • Dowling E J, Chander C L, Claxson A W, Lillie C, Blake DR. Assessment of human recombinant manganese superoxide dismutase in models of inflammation. Free Radic. Res. Commun. 1993; 18: 291–298
  • Mao G D, Poznansky J. Superoxide dismutase: Improving its pharmacological properties by conjugation with human serum albumin. Biomat. Art. Cells, Art. Org. 1989; 17(3)229–244
  • Milardi D, Larosa C, Grasso D. Differential scanning calorimetry of the irreversible denaturation of bovine superoxide dismutase. Thermochimica Acta 1994; 246(1)183–191
  • Inouye K, Osaki A, Tonomura B. Dissociation of dimer of bovine erythrocyte Cu, Zn-SOD and activity of the monomer subunit - Effects of Urea, temerature and enzyme concentration. J Biochem. 1994; 115(3)507–515
  • Folcarelli S, Battistoni A, Carri M T, Polricelli F, Falconi M, Nicolini L, Stella L, Rosato N, Rotilio G, Dcsideri A. Protein Engineering 1996; 9(4)323–325
  • Quebec E A, Chang I MS. Superoxide dismutase and catalase crosslinked to polyhemoglobin reduces methemoglobin formation m-vitro. Art. Cells, Blood Subs., Immob. Biotech. 1995; 25: 693–706
  • Nakaoka R, Tabata Y, Yamaoka T, Ikada Y. Prolongation of the serum half-life period of superoxide dismutase by poly(ethylene glycol) modification. J Controlled Release 1997; 46: 253–261
  • Caliceti P, Schiavon O, Hirano T, Ohashi S, Veronese FM. Modification of physico-chemical and biopharmaceutical properties of superoxide dismutase by conjugation to the copolymer of divinyl ether and maleic anhydride. J Controlled Release 1996; 39: 27–34
  • Hirano T, Todoroki T, Kato S, Yamamoto H, Caliceti P, Veronese F M, Maeda H, Ohashi S. Synthesis of the conjugate of superoxide dismutase with the copolymer of divinyl ether and maleic anhydride retaining enzymatic activity. J Controlled Release 1994; 28: 203–209
  • Caliceti P, Schiavon O, Morpurgo M, Veronese F M, Sartore L, Ranucci E, Ferruti P. Physicochemical and biological properties of monofunctional hydroxy terminating poly(N-vinylpyrrolidone) conjugated SOD. J Bioactive and Compatible polymers 1995; 10(2)103–120
  • Eryomin A N, Litvinchuk A V, Metelitza DI. Operational stability of catalase and its conjugates with aldehyde dextrans and superoxide dismutase. Biochemistry-Moscow 1996; 61(4)483–494
  • Delanian S, Baillet F, Huart J, Lefaix J L, Maulard C, Housset M. Successful treatment of radiation- Induced fibrosis using liposomal Cu/Zn superoxide dismutase - Clinical Trial. Radiotherapy and Oncology 1994; 32(1)12–20
  • Regnault C, Benoist C, Fessi H, Rocharveiiler M, Postaire E, Hazebroucq G. Preparation of superoxide dismutase entrapped in ceramide-containing liposomes for oral-administration. Inter. J. Pharmaceutics 1996; 132: 263–266; l–2
  • Zou G L, Xia L, Li P. Preparation and characterisation of superoxide dismutase soluble in organic solvents. Acta Biochimica & Biophysica Sinica 1996; 28(1)83–88
  • Zhao X B, Qian H. Influence of biopolymer onto the construction of artificial cell containing superoxide dismutase(AC-SOD). Wuhai International symposium on biomatenals and fine polymers. Wuhai, China Oct., 1995
  • Wada K, Fujibayashi Y, Yokoyama A. Copper(II)[2,3-butanedionebis(N4-methylthiosemi carbazone)], A stable superoxide dismutase-like copper complex with high membrane penetrability. Arch. Biochem. Biophysics 1994; 310(1)1–5
  • Bonomo R P, Conte E, DeGuidi G, Maccarrone G, Rizzarelli E, Vecchio G. Characterization and superoxide dismutase activity of copper(II) complexes of 6A,6X-difunctionalized beta-cyclodextnns. J Chem. Society - Dalton Transactions 1996; 23: 4351–4355
  • Misra H P, Fridovich I. The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. J Biol. Chem. 1972; 247: 3170–3175
  • Sun M, Zigman S. An improved spectrophotometnc assay for superoxide dismutase based on epinephrine autoxidation. Anal. Biochem. 1978; 90: 81–87
  • Carstensen JT. Drug stability, Principles and Practices. Marcel Dekker INC 1995; 35–40
  • Barrett A J, Starkey PM. The interaction of cc2-Macroglobulin with proteinases. Biochemical J. 1973; 133: 709–724
  • Legres L G, Pochon F, Barray M, Gay F, Chouaib S, Delain E. Evidence for the binding of a biologically active interleukin-2 to human oc2-Macroglobulin. J Biological Chemistry 1995; 279(15)8381–8384
  • Tai T, Yamashita K, Ogata-Arakawa M, Koide N, Muramatsu T, Iwashita S, Inoue Y, Kobata A. Structural studies of two ovalbumin glycopeptides in relation to the endo-beta-N-acetylglucosaminidase specificity. J Biol. Chem. 1975; 250(21)8569–8575
  • Huber W, Saifer M GP. Orgetein, the drug version of bovine Cu, Zn-Superoxide dismutase. Superoxide and superoxide dismutase, AM Michelson, JM McCord, I. Fridovich. Academic Press., London 1984; 518
  • Eastbum S D, Tao BY. Application of modified cyclodextrins. Biotech. Adv. 1994; 12: 325–339
  • Lane M. Is sugar the secret of more stable drugs. Manufacturing Chemist 1995; 66(11)32–33

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