메뉴 건너뛰기




Volumn 98, Issue 4, 1996, Pages 753-758

Purification and characterization of UDP-D-galactose 4-epimerase from the red alga Galdieria sulphuraria

Author keywords

Galdieria sulphuraria; Properties; Purification; Rhodophyta; UDP D galactose 4 epimerase

Indexed keywords

ALGAE; GALDIERIA SULPHURARIA; RHODOPHYTA;

EID: 0030433256     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1399-3054.1996.tb06681.x     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 0014390445 scopus 로고
    • The chemical composition of isolated cell walls of Cyanidium caldarium
    • Bailey, R. W. & Staehelin, L. A. 1968. The chemical composition of isolated cell walls of Cyanidium caldarium. - J. Gen. Microbiol. 54: 269-276.
    • (1968) J. Gen. Microbiol. , vol.54 , pp. 269-276
    • Bailey, R.W.1    Staehelin, L.A.2
  • 2
    • 0015187989 scopus 로고
    • The synthesis of L-galactose by plant enzyme systems
    • Barber, G. A. 1971. The synthesis of L-galactose by plant enzyme systems. - Arch. Biochem. Biophys. 147: 619-623.
    • (1971) Arch. Biochem. Biophys. , vol.147 , pp. 619-623
    • Barber, G.A.1
  • 3
    • 0009877782 scopus 로고
    • Verlag Chemie, Weinheim, Germany. ISBN 3-527-26043-9
    • Bergmeyer, H. U. (Ed.). 1983. Methods of Enzymatic Analysis (3rd Ed.), Vol. 3, pp. 171-175, 277-283, 286-293. Verlag Chemie, Weinheim, Germany. ISBN 3-527-26043-9.
    • (1983) Methods of Enzymatic Analysis (3rd Ed.) , vol.3 , pp. 171-175
    • Bergmeyer, H.U.1
  • 4
    • 84988074679 scopus 로고
    • Improved silver staining for plant proteins, RNA, and DNA in polyacrylamide gels
    • Blum, H., Beier, H. & Gross, H. J. 1987. Improved silver staining for plant proteins, RNA, and DNA in polyacrylamide gels. - Electrophoresis 8: 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. - Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0344058239 scopus 로고
    • Uridine diphosphogalactose-4 épimérase de fenugrec: Essais de purification et quelques properstes
    • Clermont, S. & Percheron, F. 1979. Uridine diphosphogalactose-4 épimérase de fenugrec: Essais de purification et quelques properstes. - Phytochemistry 18: 1963-1965.
    • (1979) Phytochemistry , vol.18 , pp. 1963-1965
    • Clermont, S.1    Percheron, F.2
  • 7
    • 0017774496 scopus 로고
    • Changes in enzymic activities of nucleoside diphosphate sugar interconversions during differentiation of cambium to xylem in pine and fir
    • Dalessandro, G. & Northcote, D. H. 1977a. Changes in enzymic activities of nucleoside diphosphate sugar interconversions during differentiation of cambium to xylem in pine and fir. - Biochem. J. 162: 281-288.
    • (1977) Biochem. J. , vol.162 , pp. 281-288
    • Dalessandro, G.1    Northcote, D.H.2
  • 8
    • 0017774540 scopus 로고
    • Changes in enzymic activities of nucleoside diphosphate sugar interconversions during differentiation of cambium to xylem in sycamore and poplar
    • - & Northcote, D. H. 1977b. Changes in enzymic activities of nucleoside diphosphate sugar interconversions during differentiation of cambium to xylem in sycamore and poplar. -Biochem. J. 162: 267-279.
    • (1977) Biochem. J. , vol.162 , pp. 267-279
    • Northcote, D.H.1
  • 9
    • 0001784247 scopus 로고
    • Possible control sites of polysaccharide synthesis during cell growth and wall expansion of pea seedlings
    • - & Northcote, D. H. 1977c. Possible control sites of polysaccharide synthesis during cell growth and wall expansion of pea seedlings. - Planta 134: 39-44.
    • (1977) Planta , vol.134 , pp. 39-44
    • Northcote, D.H.1
  • 10
    • 0013396352 scopus 로고
    • UDP-galactose 4′-epimerase from Vicia faba seeds
    • Dey, P. M. 1984. UDP-galactose 4′-epimerase from Vicia faba seeds. - Photochemistry 23: 729-732.
    • (1984) Photochemistry , vol.23 , pp. 729-732
    • Dey, P.M.1
  • 12
    • 0016167076 scopus 로고
    • The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters
    • Eisenthal, R. & Cornish-Bowden, A. 1974. The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. - Biochem. J. 139: 715-720.
    • (1974) Biochem. J. , vol.139 , pp. 715-720
    • Eisenthal, R.1    Cornish-Bowden, A.2
  • 13
    • 0000642736 scopus 로고
    • Nucleoside diphosphate-sugar 4-epimerases. I. Uridine diphosphate glucose 4-epimerase of wheat germ
    • Fan, D.-F. & Feingold, D. S. 1969. Nucleoside diphosphate-sugar 4-epimerases. I. Uridine diphosphate glucose 4-epimerase of wheat germ. - Plant Physiol. 44: 599-604.
    • (1969) Plant Physiol. , vol.44 , pp. 599-604
    • Fan, D.-F.1    Feingold, D.S.2
  • 14
    • 0018792048 scopus 로고
    • Ribulose 1,5-bisphosphate carboxylase from the thermophilic, acidophilic alga Cyanidium caldarium Geitler. Purification, characterisation and thermostability of the enzyme
    • Ford, T. W. 1979. Ribulose 1,5-bisphosphate carboxylase from the thermophilic, acidophilic alga Cyanidium caldarium Geitler. Purification, characterisation and thermostability of the enzyme. - Biochim. Biophys. Acta 569: 239-248.
    • (1979) Biochim. Biophys. Acta , vol.569 , pp. 239-248
    • Ford, T.W.1
  • 15
    • 0018855448 scopus 로고
    • The enzymes of the galactose cluster in Saccharomyces cerevisiae. II. Purification and characterization of undine diphosphoglucose 4-epimerase
    • Fukasawa, T., Obonai, K., Segawa, T. & Nogi, Y. 1980. The enzymes of the galactose cluster in Saccharomyces cerevisiae. II. Purification and characterization of undine diphosphoglucose 4-epimerase. - J. Biol. Chem. 255: 2705-2707.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2705-2707
    • Fukasawa, T.1    Obonai, K.2    Segawa, T.3    Nogi, Y.4
  • 16
    • 0017359133 scopus 로고
    • Purification and characterization of UDP-galactose-4-epimerase from bovine tissue
    • Geren, C. R. & Ebner, K. E. 1977. Purification and characterization of UDP-galactose-4-epimerase from bovine tissue. - J. Biol. Chem. 252: 2082-2088.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2082-2088
    • Geren, C.R.1    Ebner, K.E.2
  • 17
    • 0001305431 scopus 로고
    • Membrane-bound malate dehydrogenase in mitochondria from the alga Cyanidium caldarium
    • Gross, W. 1990. Membrane-bound malate dehydrogenase in mitochondria from the alga Cyanidium caldarium. - Phytochemistry 29: 3081-3085.
    • (1990) Phytochemistry , vol.29 , pp. 3081-3085
    • Gross, W.1
  • 18
    • 0028851273 scopus 로고
    • Heterotrophic growth of two strains of the acido-thermophilic red alga Galdieria sulphuraria
    • - & Schnarrenberger, C. 1995. Heterotrophic growth of two strains of the acido-thermophilic red alga Galdieria sulphuraria. - Plant Cell Physiol. 36: 633-638.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 633-638
    • Schnarrenberger, C.1
  • 19
    • 0004072425 scopus 로고
    • John Wiley & Sons, London, ISBN 0-471-33715-3
    • Gutfreund, H. (ed.). 1972. Enzymes: Physical Principles. - John Wiley & Sons, London, pp. 161-162. ISBN 0-471-33715-3.
    • (1972) Enzymes: Physical Principles , pp. 161-162
    • Gutfreund, H.1
  • 20
    • 0344058237 scopus 로고
    • Turnover of galactosylglycerol and osmotic balance in Ochromonas
    • Kauss, H. 1973. Turnover of galactosylglycerol and osmotic balance in Ochromonas. - Plant Physiol. 52: 613-615.
    • (1973) Plant Physiol. , vol.52 , pp. 613-615
    • Kauss, H.1
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bactenophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bactenophage T4. - Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0015994146 scopus 로고
    • Interaction of nucleotides with liver uridine diphosphate glucose-4′-epimerase
    • Langer, R. & Glaser, L. 1974. Interaction of nucleotides with liver uridine diphosphate glucose-4′-epimerase. - J. Biol. Chem. 249: 1126-1132.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1126-1132
    • Langer, R.1    Glaser, L.2
  • 23
    • 0000991235 scopus 로고
    • Characteristics of a galactose-adapted sugarcane cell line grown in suspension culture
    • Maretzki, A. & Thom, M. 1978. Characteristics of a galactose-adapted sugarcane cell line grown in suspension culture. -Plant Physiol. 61: 544-548.
    • (1978) Plant Physiol. , vol.61 , pp. 544-548
    • Maretzki, A.1    Thom, M.2
  • 24
    • 73049130725 scopus 로고
    • A method for determining the sedimentation behavior of enzymes: Application to protein mixtures
    • Martin, R. G. & Ames, B. N. 1961. A method for determining the sedimentation behavior 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
  • 25
    • 0000451294 scopus 로고
    • The enzymatic interconversion of uridine diphosphogalactose and uridine diphosphoglucose
    • Maxwell, E. S. 1957. The enzymatic interconversion of uridine diphosphogalactose and uridine diphosphoglucose. - J. Biol. Chem. 229: 139-151.
    • (1957) J. Biol. Chem. , vol.229 , pp. 139-151
    • Maxwell, E.S.1
  • 26
    • 0005889953 scopus 로고
    • Purification of uridine diphosphate galactose-4-epimerase from yeast, and the identification of protein-bound diphosphopyridine nucleotide
    • - & de Robichon-Szulmajster, H. 1960. Purification of uridine diphosphate galactose-4-epimerase from yeast, and the identification of protein-bound diphosphopyridine nucleotide. -J. Biol. Chem. 235: 308-312.
    • (1960) J. Biol. Chem. , vol.235 , pp. 308-312
    • De Robichon-Szulmajster, H.1
  • 27
    • 0015632075 scopus 로고
    • The formation of a β-(1-4)-D-galactan chain catalyzed by a Phaseolus aureus enzyme
    • Panayatotos, N. & Villemez, C. L. 1973. The formation of a β-(1-4)-D-galactan chain catalyzed by a Phaseolus aureus enzyme. - Biochem. J. 133: 263-271.
    • (1973) Biochem. J. , vol.133 , pp. 263-271
    • Panayatotos, N.1    Villemez, C.L.2
  • 28
    • 0000625712 scopus 로고
    • Taxonomic implications of osmoacclimation in Cyanidium caldarium (Tilden) Geitler
    • Reed, R. H. 1983. Taxonomic implications of osmoacclimation in Cyanidium caldarium (Tilden) Geitler. - Phycoloeia 22: 351-354.
    • (1983) Phycoloeia , vol.22 , pp. 351-354
    • Reed, R.H.1
  • 29
    • 0013405438 scopus 로고
    • The activity of uridine diphosphate-D-glucose-4-epimerase in cambial tissue and differentiating xylena isolated from sycamore (Acer pseudoplatanus) trees
    • Rubery, P. H. 1973. The activity of uridine diphosphate-D-glucose-4-epimerase in cambial tissue and differentiating xylena isolated from sycamore (Acer pseudoplatanus) trees. -Planta 111: 267-269.
    • (1973) Planta , vol.111 , pp. 267-269
    • Rubery, P.H.1
  • 30
    • 0015548474 scopus 로고
    • Two isoenzymes each of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in spinach leaves
    • Schnarrenberger, C., Oeser, A. & Tolbert, N. E. 1973. Two isoenzymes each of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in spinach leaves. - Arch. Biochem. Biophys. 154: 438-448.
    • (1973) Arch. Biochem. Biophys. , vol.154 , pp. 438-448
    • Schnarrenberger, C.1    Oeser, A.2    Tolbert, N.E.3
  • 31
    • 0000677607 scopus 로고
    • Carbohydrates and nucleotides in the red alga Porphyra perforata. I. Isolation and identification of carbohydrates
    • Su, J. C. & Hassid, W. Z. 1962. Carbohydrates and nucleotides in the red alga Porphyra perforata. I. Isolation and identification of carbohydrates. - Biochemistry 1: 468-474.
    • (1962) Biochemistry , vol.1 , pp. 468-474
    • Su, J.C.1    Hassid, W.Z.2
  • 32
    • 0001678581 scopus 로고
    • UDP-glucose-4-epimerase from Poterioochromonas mathamensis
    • Thomson, K. S., Jung, C. & Kauss, H. 1984. UDP-glucose-4-epimerase from Poterioochromonas mathamensis. - Phytochemistry 23: 979-981.
    • (1984) Phytochemistry , vol.23 , pp. 979-981
    • Thomson, K.S.1    Jung, C.2    Kauss, H.3
  • 33
    • 0014708095 scopus 로고
    • Purification, stabilization, and properties of bovine mammary UDP-galactose 4-epimerase
    • Tsai, C. M., Holmberg, N. & Ebner, K. E. 1970. Purification, stabilization, and properties of bovine mammary UDP-galactose 4-epimerase. - Arch. Biochem. Biophys. 136: 233-244.
    • (1970) Arch. Biochem. Biophys. , vol.136 , pp. 233-244
    • Tsai, C.M.1    Holmberg, N.2    Ebner, K.E.3
  • 34
    • 0000745994 scopus 로고
    • Isolierung und Kristallisation des Gärungsferments Enolase
    • Warburg, O. & Christian, W. 1941. Isolierung und Kristallisation des Gärungsferments Enolase. - Biochem. Z. 310: 384-421.
    • (1941) Biochem. Z. , vol.310 , pp. 384-421
    • Warburg, O.1    Christian, W.2
  • 35
    • 0000290994 scopus 로고
    • The enzymes of the galactose operon in Escherichia coli. I. Purification and characterization of uridine diphosphogalactose 4-epimerase
    • Wilson, D. B. & Hogness, D. S. 1964. The enzymes of the galactose operon in Escherichia coli. I. Purification and characterization of uridine diphosphogalactose 4-epimerase. - J. Biol. Chem. 239: 2469-2481.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2469-2481
    • Wilson, D.B.1    Hogness, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.