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Volumn 62, Issue 7, 1996, Pages 2586-2592

Purification by immunoaffinity chromatography, characterization, and structural analysis of a thermostable pyranose oxidase from the white rot fungus Phlebiopsis gigantea

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; OXIDOREDUCTASE; PYRANOSIDE;

EID: 0029908625     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.62.7.2586-2592.1996     Document Type: Article
Times cited : (43)

References (42)
  • 1
    • 0000694228 scopus 로고
    • Molecular weight estimations of proteins by electrophoresis in polyacrylamide gels of graded porosity
    • Andersson, L. O., H. Borg, and M. Mikaelsson. 1972. Molecular weight estimations of proteins by electrophoresis in polyacrylamide gels of graded porosity. FEBS Lett. 20:199-202.
    • (1972) FEBS Lett. , vol.20 , pp. 199-202
    • Andersson, L.O.1    Borg, H.2    Mikaelsson, M.3
  • 2
    • 0018884529 scopus 로고
    • Inhibition of protein synthesis in vitro by proteins from the seeds of Momordica charantia (bitter pear melon)
    • Barbieri, L., M. Zamboni, E. Lorenzoni, L. Montanaro, S. Sperti, and F. Stirpe. 1980. Inhibition of protein synthesis in vitro by proteins from the seeds of Momordica charantia (bitter pear melon). Biochem. J. 186:443-452.
    • (1980) Biochem. J. , vol.186 , pp. 443-452
    • Barbieri, L.1    Zamboni, M.2    Lorenzoni, E.3    Montanaro, L.4    Sperti, S.5    Stirpe, F.6
  • 3
    • 0015515033 scopus 로고
    • Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Purification and properties of D-6-hydroxynicotine oxidase
    • Brühmüller, M., H. Möhler, and K. Decker. 1972. Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Purification and properties of D-6-hydroxynicotine oxidase. Eur. J. Biochem. 29:143-151.
    • (1972) Eur. J. Biochem. , vol.29 , pp. 143-151
    • Brühmüller, M.1    Möhler, H.2    Decker, K.3
  • 4
    • 0028340896 scopus 로고
    • 2 during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida
    • 2 during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida. Appl. Environ. Microbiol. 60:2524-2532.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2524-2532
    • Daniel, G.1    Vole, J.2    Kubatova, E.3
  • 5
    • 0028324235 scopus 로고
    • Production, purification and characterization of an alcohol oxidase from the ligninolytic fungus Peniophora gigantea
    • Danneel, H. J., A. Reichert, and F. Giffhorn. 1994. Production, purification and characterization of an alcohol oxidase from the ligninolytic fungus Peniophora gigantea. J. Biotechnol. 33:33-41.
    • (1994) J. Biotechnol. , vol.33 , pp. 33-41
    • Danneel, H.J.1    Reichert, A.2    Giffhorn, F.3
  • 6
    • 0027310313 scopus 로고
    • Purification and characterization of a pyranose oxidase from the basidiomycete Peniophora gigantea and chemical analysis of its reaction products
    • Danneel, H. J., E. Rössner, A. Zeeck, and F. Giffhorn. 1993. Purification and characterization of a pyranose oxidase from the basidiomycete Peniophora gigantea and chemical analysis of its reaction products. Eur. J. Biochem. 214: 795-802.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 795-802
    • Danneel, H.J.1    Rössner, E.2    Zeeck, A.3    Giffhorn, F.4
  • 7
    • 0026955806 scopus 로고
    • Goal-oriented screening method for carbohydrate oxidases produced by filamentous fungi
    • Danneel, H. J., M. Ullrich, and F. Giffhorn. 1992. Goal-oriented screening method for carbohydrate oxidases produced by filamentous fungi. Enzyme Microb. Technol. 14:898-903.
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 898-903
    • Danneel, H.J.1    Ullrich, M.2    Giffhorn, F.3
  • 8
    • 0017990368 scopus 로고
    • Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-Sepharose
    • Ey, P. L., S. J. Prowse, and C. R. Jenkin. 1978. Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-Sepharose. Immunochemistry 15:429-436.
    • (1978) Immunochemistry , vol.15 , pp. 429-436
    • Ey, P.L.1    Prowse, S.J.2    Jenkin, C.R.3
  • 10
    • 0028069399 scopus 로고
    • A convenient laboratory procedure for the preparation of cortalcerone, a fungal antibiotic β-pyrone
    • Gabriel, J., J. Volc, E. Kubatova, Z. Palkova, and M. Pospisck. 1994. A convenient laboratory procedure for the preparation of cortalcerone, a fungal antibiotic β-pyrone. Carhohydr. Res. 252:297-3111.
    • (1994) Carhohydr. Res. , vol.252 , pp. 297-3111
    • Gabriel, J.1    Volc, J.2    Kubatova, E.3    Palkova, Z.4    Pospisck, M.5
  • 11
    • 0017832443 scopus 로고
    • The lectins: Carbohydrate-binding proteins of plants and animals
    • Goldstein, I. J., and C. E. Hayes. 1978. The lectins: carbohydrate-binding proteins of plants and animals. Adv. Carbohydr. Chem. Biochem. 35:127-340.
    • (1978) Adv. Carbohydr. Chem. Biochem. , vol.35 , pp. 127-340
    • Goldstein, I.J.1    Hayes, C.E.2
  • 12
    • 0028208570 scopus 로고
    • Laboratory procedures for producing 2-keto-D-glucose, 2-keto-D-xylose, and 5-keto-D-fructose from D-glucose, D-xylose, and L-sorbose with immobilized pyranose oxidase of Peniophora gigantea
    • Huwig, A., H.-J. Danneel, and F. Giffhorn. 1994. Laboratory procedures for producing 2-keto-D-glucose, 2-keto-D-xylose, and 5-keto-D-fructose from D-glucose, D-xylose, and L-sorbose with immobilized pyranose oxidase of Peniophora gigantea. J. Biotechnol. 32:309-315.
    • (1994) J. Biotechnol. , vol.32 , pp. 309-315
    • Huwig, A.1    Danneel, H.-J.2    Giffhorn, F.3
  • 13
    • 0001280226 scopus 로고
    • Isolation of a new pyranose oxidase producing basidiomycete
    • Izumi, Y., Y. Furuya, and H. Yamada. 1990. Isolation of a new pyranose oxidase producing basidiomycete. Agric. Biol. Chem. 54:799-801.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 799-801
    • Izumi, Y.1    Furuya, Y.2    Yamada, H.3
  • 14
    • 0000311402 scopus 로고
    • Purification and properties of pyranose oxidase from basidiomycetous fungus no. 52
    • Izumi, Y., Y. Furuya, and H. Yamada. 1990. Purification and properties of pyranose oxidase from basidiomycetous fungus no. 52. Agric. Biol. Chem. 54: 1393-1399.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 1393-1399
    • Izumi, Y.1    Furuya, Y.2    Yamada, H.3
  • 15
    • 0016417590 scopus 로고
    • Pyranose oxidase from Polyporus obtusus
    • Janssen, F. W., and H. W. Ruelius. 1975. Pyranose oxidase from Polyporus obtusus. Methods Enzymol. 41:170-173.
    • (1975) Methods Enzymol. , vol.41 , pp. 170-173
    • Janssen, F.W.1    Ruelius, H.W.2
  • 17
    • 0026898199 scopus 로고
    • Synthesis of the antibiotic cortalcerone from D-glucosc using pyranose oxidase and a novel fungal enzyme, aldos-2-ulose dehydratase
    • Koths, K., R. Halenbeck, and M. Moreland. 1992. Synthesis of the antibiotic cortalcerone from D-glucosc using pyranose oxidase and a novel fungal enzyme, aldos-2-ulose dehydratase. Carhohydr. Res. 232:59-75.
    • (1992) Carhohydr. Res. , vol.232 , pp. 59-75
    • Koths, K.1    Halenbeck, R.2    Moreland, M.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0000302766 scopus 로고
    • Convenient laboratory procedure for producing solid D-arabino-hexos-2-ulose (D-glucosone)
    • Liu, T.-N. E., B. Wolf, J. Geigert, S. L. Neidleman, J. D. Chin, and D. S. Hirano. 1983. Convenient laboratory procedure for producing solid D-arabino-hexos-2-ulose (D-glucosone). Carbohydr. Res. 113:151-157.
    • (1983) Carbohydr. Res. , vol.113 , pp. 151-157
    • Liu, T.-N.E.1    Wolf, B.2    Geigert, J.3    Neidleman, S.L.4    Chin, J.D.5    Hirano, D.S.6
  • 22
    • 84954938061 scopus 로고
    • Purification and properties of pyranose oxidase from Coriolus versicolor
    • Machida, Y., and T. Nakanishi. 1984. Purification and properties of pyranose oxidase from Coriolus versicolor. Agric. Biol. Chem. 48:2463-2470.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 2463-2470
    • Machida, Y.1    Nakanishi, T.2
  • 23
    • 73049130725 scopus 로고
    • A method for determining the sedimentation behaviour of enzymes: Application to protein mixtures
    • Martin, R. G., and B. N. Ames. 1961. A method for determining the sedimentation behaviour of enzymes: application to protein mixtures. J. Biol. Chem. 236:1372-1379.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1372-1379
    • Martin, R.G.1    Ames, B.N.2
  • 24
    • 0019492995 scopus 로고
    • Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins
    • Merril, C. R., D. Goldman, S. A. Sedman, and M. H. Ebert. 1981. Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins. Science 211:1437-1438.
    • (1981) Science , vol.211 , pp. 1437-1438
    • Merril, C.R.1    Goldman, D.2    Sedman, S.A.3    Ebert, M.H.4
  • 25
    • 84981776413 scopus 로고
    • Antigen-antibody reactions in gels, types of reactions in coordinated systems of diffusion
    • Ouchterlony, Ö. 1953. Antigen-antibody reactions in gels, types of reactions in coordinated systems of diffusion. Acta Pathol. Microbiol. Scand. 32:231-240.
    • (1953) Acta Pathol. Microbiol. Scand. , vol.32 , pp. 231-240
    • Ouchterlony, Ö.1
  • 26
    • 8544279414 scopus 로고
    • Control of 8-bromo-AMP and 8-(6-aminohexyl)amino-AMP synthesis by HPLC
    • Raffin, J. P., and C. Leray. 1980. Control of 8-bromo-AMP and 8-(6-aminohexyl)amino-AMP synthesis by HPLC. J. Chromatogr. 196:323-330.
    • (1980) J. Chromatogr. , vol.196 , pp. 323-330
    • Raffin, J.P.1    Leray, C.2
  • 27
    • 0001229625 scopus 로고
    • Selective oxidation of D-glucose: Chiral intermediates for industrial utilization
    • F. W. Liehtenthaler (ed.), Verlag Chemie, Weinheim, Germany
    • Röper, H. 1991. Selective oxidation of D-glucose: chiral intermediates for industrial utilization, p. 267-288. In F. W. Liehtenthaler (ed.), Carbohydrates as organic raw materials. Verlag Chemie, Weinheim, Germany.
    • (1991) Carbohydrates As Organic Raw Materials , pp. 267-288
    • Röper, H.1
  • 30
    • 30344463700 scopus 로고
    • Molecular weight determination of glycoproteins by polyacrylamide gel electrophoresis in sodium dodecyl sulfate
    • Segrest, J. P., and R. L. Jackson. 1972. Molecular weight determination of glycoproteins by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Methods Enzymol. 28:54-63.
    • (1972) Methods Enzymol. , vol.28 , pp. 54-63
    • Segrest, J.P.1    Jackson, R.L.2
  • 31
    • 0000311409 scopus 로고
    • Stabilization of pyranose-2-oxidase and catalase by chemical modification
    • Shaked, Z., and S. Wolfe. 1988. Stabilization of pyranose-2-oxidase and catalase by chemical modification. Methods Enzymol. 137:599-615.
    • (1988) Methods Enzymol. , vol.137 , pp. 599-615
    • Shaked, Z.1    Wolfe, S.2
  • 32
    • 0027209952 scopus 로고
    • Purification and characterization of D-glucose oxidase from white-rot fungus Pleurotus ostreatus
    • Shin, K.-S., H.-D. Youn, Y.-H. Han, S.-O. Kang, and Y. C. Hah. 1993. Purification and characterization of D-glucose oxidase from white-rot fungus Pleurotus ostreatus. Eur. J. Biochem. 215:747-752.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 747-752
    • Shin, K.-S.1    Youn, H.-D.2    Han, Y.-H.3    Kang, S.-O.4    Hah, Y.C.5
  • 33
    • 0014007813 scopus 로고
    • Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases
    • Siegel, L. M., and K. J. Monty. 1966. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases. Biochim. Biophys. Acta 112:346-362.
    • (1966) Biochim. Biophys. Acta , vol.112 , pp. 346-362
    • Siegel, L.M.1    Monty, K.J.2
  • 34
    • 0000475128 scopus 로고
    • Purification and properties of glucose oxidase from Aspergillus niger
    • Swoboda, B. E. P., and V. Massey. 1965. Purification and properties of glucose oxidase from Aspergillus niger. J. Biol. Chem. 240:2209-2215.
    • (1965) J. Biol. Chem. , vol.240 , pp. 2209-2215
    • Swoboda, B.E.P.1    Massey, V.2
  • 35
    • 0006665893 scopus 로고
    • Glucose-2-oxidase (Coriolus versicolor) and its application to D-glucose colorimetry
    • Taguchi, T., K. Ohwaki, and J. Okuda. 1985. Glucose-2-oxidase (Coriolus versicolor) and its application to D-glucose colorimetry. J. Appl. Biochem. 7:289-295.
    • (1985) J. Appl. Biochem. , vol.7 , pp. 289-295
    • Taguchi, T.1    Ohwaki, K.2    Okuda, J.3
  • 36
    • 0014301425 scopus 로고
    • Regulation of glutamate synthetase. XII. Electron microscopy of the enzyme from Escherichia coli
    • Valentine, R. C., B. M. Shapiro, and E. R. Stadtman. 1968. Regulation of glutamate synthetase. XII. Electron microscopy of the enzyme from Escherichia coli. Biochemistry 7:2143-2152.
    • (1968) Biochemistry , vol.7 , pp. 2143-2152
    • Valentine, R.C.1    Shapiro, B.M.2    Stadtman, E.R.3
  • 37
    • 0025743295 scopus 로고
    • Pyranose oxidase and pyranosone dehydratase: Enzymes responsible for conversion of D-glucose to cortalcerone by the basidiomycete Phanerochaete chrysosporium
    • Volc, J., E. Kubatova, P. Sedmera, G. Daniel, and J. Gabriel. 1991. Pyranose oxidase and pyranosone dehydratase: enzymes responsible for conversion of D-glucose to cortalcerone by the basidiomycete Phanerochaete chrysosporium. Arch. Microbiol. 156:297-301.
    • (1991) Arch. Microbiol. , vol.156 , pp. 297-301
    • Volc, J.1    Kubatova, E.2    Sedmera, P.3    Daniel, G.4    Gabriel, J.5
  • 38
    • 0028973477 scopus 로고
    • Conversion of D-glucose to D-erythro-hexos-2,3-diulose(2,3-diketo-D-glucose) by enzyme preparations from the basidiomycete Oudemansiella mucida
    • Volc, J., P. Sedmera, V. Havlicek, V. Prikrylova, and G. Daniel. 1995. Conversion of D-glucose to D-erythro-hexos-2,3-diulose(2,3-diketo-D-glucose) by enzyme preparations from the basidiomycete Oudemansiella mucida. Carbohydr. Res. 278:59-70.
    • (1995) Carbohydr. Res. , vol.278 , pp. 59-70
    • Volc, J.1    Sedmera, P.2    Havlicek, V.3    Prikrylova, V.4    Daniel, G.5
  • 39
    • 0024463236 scopus 로고
    • Simple enzymatic method for determining 1,5-anhydro-D-glucitol in plasma for diagnosis of diabetes mellitus
    • Yabuuchi, M., M. Masuda, K. Katoh, T. Nakamura, and H. Akanuma. 1989. Simple enzymatic method for determining 1,5-anhydro-D-glucitol in plasma for diagnosis of diabetes mellitus. Clin. Chem. 35:2039-2043.
    • (1989) Clin. Chem. , vol.35 , pp. 2039-2043
    • Yabuuchi, M.1    Masuda, M.2    Katoh, K.3    Nakamura, T.4    Akanuma, H.5
  • 40
    • 0000307813 scopus 로고
    • Properties of choline oxidase of Cylindrocarpon didymum M-1
    • Yamada, H., N. Mori, and Y. Tani. 1979. Properties of choline oxidase of Cylindrocarpon didymum M-1. Agric. Biol. Chem. 43:2173-2177.
    • (1979) Agric. Biol. Chem. , vol.43 , pp. 2173-2177
    • Yamada, H.1    Mori, N.2    Tani, Y.3
  • 41
    • 0015056896 scopus 로고
    • Subunit structure of glucose oxidase from Penicillium amagasakiense
    • Yoshimura, T., and T. Isemura. 1971. Subunit structure of glucose oxidase from Penicillium amagasakiense. J. Biochem. 69:839-846.
    • (1971) J. Biochem. , vol.69 , pp. 839-846
    • Yoshimura, T.1    Isemura, T.2
  • 42
    • 0014981447 scopus 로고
    • An X-ray small angle study of bacteriophages fr and R17
    • Zipper, P., O. Kratky, R. Herrmenn, and T. Hohn. 1971. An X-ray small angle study of bacteriophages fr and R17. Eur. J. Biochem. 18:1-9
    • (1971) Eur. J. Biochem. , vol.18 , pp. 1-9
    • Zipper, P.1    Kratky, O.2    Herrmenn, R.3    Hohn, T.4


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