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Research Article

β-D(+) Glucose-Glucose Oxidase-Catalase for Use as an Antioxidant System

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Pages 127-134 | Received 24 Oct 1995, Accepted 15 Feb 1996, Published online: 27 Sep 2008

References

  • Lachman L., DeLuca P., Akers M. J. Kinetic principles and stability testing. The Theory and Practice of Industrial Pharmacy, L. Lachman, H. A. Lieberman, J. L. Kanig. Lea and Febiger/Varghese, Bombay 1991; 780, Fourth Indian Reprint
  • Berg T. F., Niebergall P. J. Glucose oxidase as a pharmaceutical antioxidant. Drug Dev. Ind. Pharm. 1992; 18(16)1813–1822
  • , Glucose Oxidase Assay Instruction, No. 5139, 5th ed., 0076G, Boehringer Mannheim GmbH, July 1987. (Available from Kontroll-Labor Biochemie, Boehringer Mannheim Corporation, PO Box 50414, Indianapolis, IN 46250–0414, USA.)
  • , Glucose Oxidase Assay Procedure (3/88). (Available from Sigma Chemical Company, PO Box 14508, St. Louis, MO 63178, USA.)
  • Underkofler L. A. Properties and applications of the fungal enzyme glucose oxidase. Proc. Int. Symp. Enzyme Chem., Tokyo and Kyoto 1957; W-2: 486–490
  • Gibson Q. H., Swoboda B. E. P., Massey V. Kinetics and mechanism of action of glucose oxidase. J. Biol. Chem. 1964; 239(11)3927–3934
  • Ingold K. U. Peroxy radicals. Ace. Chem. Res. 1969; 2(1)1–9
  • Keilin D., Hartree E. F. Properties of glucose oxidase (Notatin). Biochem. J. 1948; 42: 221–229
  • Coulthard C. E., Michaelis R., Short W. F., Sykes G., Skrimshire G. E. H., Standfast A. F. B., Birkinshaw J. H., Raistrick H. Notatin: An antibacterial glucose-aerodehydrogenase from Penicillium notatum Westling and Penicillium resticulosum sp. nov. J. Bio-chem. 1945; 39: 24
  • Muller D. Glucose oxidase. Ergebn. Enzymforsch 1936; 5: 259
  • Ogura Y. Uber eine anoxytrope Glucosedehydrase aus Aspergillus oryzae. Untersuchungen uber die Dehydrasen von Schimmelpilzen. I. Acta. Phytochim. 1939; 11: 127
  • Nakamura T., Ogura Y. Kinetic studies on the action of glucose oxidase. J. Biochem. 1962; 52(3)214
  • Bentley R., Neuberger A. The mechanism of the action of notatin. J. Biochem. 1949; 45: 584–590
  • Chance B. The enzyme-substrate compounds of catalase and peroxides. Nature (London) 1948; 161: 914–917
  • Samejima T., Kamata M., Shibata K. Dissociation of bovine liver catalase at low pH. J. Biochem. (Tokyo) 1962; 51: 181–187
  • Valentine R. C. Sub-units of the catalase molecule seen by electron microscopy. Nature (London) 1964; 204: 1262–64
  • Kiselev A. N., Shpitzberg C. L., Vainshtein B. K. Crystallization of catalase in the form of tubes with monomolecular walls. J. Mol. Biol. 1967; 25(3)433–441
  • Sund H., Weber K., Molbert E. Dissociation of beef liver catalase into its subunits. Eur. J. Biochem. 1967; 1(4)400–410
  • Uppoor R. Kinetic evaluation and preformulation studies on β-D(+) glucose-glucose oxidase-catalase as an antioxidant system in pharmaceutical solutions, dissertation submitted to the College of Graduate Studies. Medical University of South Carolina, Charleston, SC 1995
  • Angyal S. J. The composition of reducing sugars in solution, Table V. Asymmetry in Carbohydrates, R. E. Harmon. Marcel Dekker, New York 1979; 27
  • Sigma Chemical Company Product Catalog. Bio-chemicals, Organic Compounds for Research and Diagnostic Reagents. Sigma, St. Louis, MO 1994; 478–479

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