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Volumn 93, Issue 1, 2013, Pages 31-37

Synthesis of branched polysaccharides with tunable degree of branching

Author keywords

Degree of branching; Glycogen branching enzyme; Phosphorylase; Polysaccharides

Indexed keywords

BRANCHING ENZYME; BRANCHING POINTS; DEGREE OF BRANCHING; GLUCOSE 1-PHOSPHATE; IN-VITRO; PH VALUE; PHOSPHORYLASE; REACTION CONDITIONS; TANDEM REACTION;

EID: 84874650860     PISSN: 01448617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carbpol.2012.04.008     Document Type: Conference Paper
Times cited : (48)

References (34)
  • 1
    • 0026033985 scopus 로고
    • Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP
    • D. Barford, S.-H. Hu, and L.N. Johnson Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP Journal of Molecular Biology 218 1991 233 260
    • (1991) Journal of Molecular Biology , vol.218 , pp. 233-260
    • Barford, D.1    Hu, S.-H.2    Johnson, L.N.3
  • 2
    • 0017404313 scopus 로고
    • Biosynthesis of bacterial glycogen. purification and properties of the Escherichia coli B α-1,4-glucan:α-1,4-glucan 6-glycosyltransferase
    • C. Boyer, and J. Preiss Biosynthesis of bacterial glycogen. purification and properties of the Escherichia coli B α-1,4-glucan:α-1,4-glucan 6-glycosyltransferase Biochemistry 16 1977 3693 3699
    • (1977) Biochemistry , vol.16 , pp. 3693-3699
    • Boyer, C.1    Preiss, J.2
  • 3
    • 0016786822 scopus 로고
    • Purification and properties of rabbit liver phosphorylase phosphatase
    • H. Brandt, Z.L. Cafwlong, and E.C. Lee Purification and properties of rabbit liver phosphorylase phosphatase Journal of Biological Chemistry 20 1975 8038 8044
    • (1975) Journal of Biological Chemistry , vol.20 , pp. 8038-8044
    • Brandt, H.1    Cafwlong, Z.L.2    Lee, E.C.3
  • 4
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • D.M. Byler, and H. Susi Examination of the secondary structure of proteins by deconvolved FTIR spectra Biopolymers 25 1986 469 487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 5
    • 33947482089 scopus 로고
    • Dithiothreitol, a new protective reagent for SH groups
    • W.W. Clealand Dithiothreitol, a new protective reagent for SH groups Biochemistry 3 1964 480 482
    • (1964) Biochemistry , vol.3 , pp. 480-482
    • Clealand, W.W.1
  • 7
    • 0009316776 scopus 로고
    • The activating effect of glycogen on the enzymatic synthesis of glycogen from glucose-1-phosphate
    • G.T. Cori, and C.F. Cori The activating effect of glycogen on the enzymatic synthesis of glycogen from glucose-1-phosphate Journal of Biological Chemistry 131 1939 397
    • (1939) Journal of Biological Chemistry , vol.131 , pp. 397
    • Cori, G.T.1    Cori, C.F.2
  • 8
    • 0001529883 scopus 로고
    • The kinetics of the enzymatic synthesis of glycogen from glucose-1-phosphate
    • G.T. Cori, and C.F. Cori The kinetics of the enzymatic synthesis of glycogen from glucose-1-phosphate Journal of Biological Chemistry 135 1940 733
    • (1940) Journal of Biological Chemistry , vol.135 , pp. 733
    • Cori, G.T.1    Cori, C.F.2
  • 9
    • 0017577049 scopus 로고
    • 31P nuclear magnetic resonance studies of glycogen phosphorylase from rabbit skeletal muscle: Ionization states of pyridoxal 5′-phosphate
    • 31P nuclear magnetic resonance studies of glycogen phosphorylase from rabbit skeletal muscle: Ionization states of pyridoxal 5′-phosphate Biochemistry 74 1977 856 860
    • (1977) Biochemistry , vol.74 , pp. 856-860
    • Feldmann, K.1    Hull, W.E.2
  • 11
    • 0020486663 scopus 로고
    • Potato and rabbit muscle phosphorylases: Comparative studies on the structure, function and regulation of regulatory and nonregulatory enzymes
    • T. Fukui, S. Shimomura, and K. Nakano Potato and rabbit muscle phosphorylases: Comparative studies on the structure, function and regulation of regulatory and nonregulatory enzymes Molecular and Cellular Biochemistry 42 1982 129 144
    • (1982) Molecular and Cellular Biochemistry , vol.42 , pp. 129-144
    • Fukui, T.1    Shimomura, S.2    Nakano, K.3
  • 12
    • 0033567060 scopus 로고    scopus 로고
    • A Comparison between the sulfhydryl reductants tris(2-carboxyethyl) phosphine and dithiothreitol for use in protein biochemistry
    • E.B. Getz, M. Xiao, T. Chakrabarty, R. Cooke, and P.R. Selvin A Comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry Analytical Biochemistry 273 1999 80
    • (1999) Analytical Biochemistry , vol.273 , pp. 80
    • Getz, E.B.1    Xiao, M.2    Chakrabarty, T.3    Cooke, R.4    Selvin, P.R.5
  • 13
    • 0343958758 scopus 로고
    • Specificity of uridine diphosphate glucose-glycogen glucosyltransferase
    • S.H. Goldemberg Specificity of uridine diphosphate glucose-glycogen glucosyltransferase Biochimica et Biophysica Acta 56 1962 357 359
    • (1962) Biochimica et Biophysica Acta , vol.56 , pp. 357-359
    • Goldemberg, S.H.1
  • 14
    • 0343526758 scopus 로고    scopus 로고
    • Thermal denaturation pathway of starch phosphorylase from Corynebacterium callunae: Oxyanion binding provides the glue that efficiently stabilizes the dimer structure of the protein
    • R. Griessler, S. D'Auria, F. Tanfani, and B. Nidetzky Thermal denaturation pathway of starch phosphorylase from Corynebacterium callunae: Oxyanion binding provides the glue that efficiently stabilizes the dimer structure of the protein Protein Science 9 2000
    • (2000) Protein Science , vol.9
    • Griessler, R.1    D'Auria, S.2    Tanfani, F.3    Nidetzky, B.4
  • 15
    • 0028360823 scopus 로고
    • A procedure for quantitative determination of tris(2-carboxyethyl) phosphine, an odorless reducing agent more stable and effective than dithiothreitol
    • J.C. Han, and G.Y. Han A procedure for quantitative determination of tris(2-carboxyethyl)phosphine, an odorless reducing agent more stable and effective than dithiothreitol Analytical Biochemistry 220 1994 5 10
    • (1994) Analytical Biochemistry , vol.220 , pp. 5-10
    • Han, J.C.1    Han, G.Y.2
  • 16
    • 0015835484 scopus 로고
    • A calorimetric study of the interactions between phosphorylase b and its nucleotide activators
    • H.C. Ho, and J.H. Wang A calorimetric study of the interactions between phosphorylase b and its nucleotide activators Biochemistry 23 1973 4750 4753
    • (1973) Biochemistry , vol.23 , pp. 4750-4753
    • Ho, H.C.1    Wang, J.H.2
  • 19
    • 9144265007 scopus 로고    scopus 로고
    • Glucan synthesis in the genus Lactobacillus: Isolation and characterization of glucansucrase genes, enzymes and glucan products from six different strains
    • S. Kralj, G.H. van Geel-Schutten, M.M.G. Dondorff, S. Kirsanovs, M.J.E.C. van der Maarel, and L. Dijkhuizen Glucan synthesis in the genus Lactobacillus: Isolation and characterization of glucansucrase genes, enzymes and glucan products from six different strains Microbiology 150 2004 3681 3690
    • (2004) Microbiology , vol.150 , pp. 3681-3690
    • Kralj, S.1    Van Geel-Schutten, G.H.2    Dondorff, M.M.G.3    Kirsanovs, S.4    Van Der Maarel, M.J.E.C.5    Dijkhuizen, L.6
  • 20
    • 79952616677 scopus 로고    scopus 로고
    • Rate coefficients for enzyme-catalyzed reactions from molecular weight distributions
    • W.-C. Liu, J.V. Castro, and R.G. Gilbert Rate coefficients for enzyme-catalyzed reactions from molecular weight distributions Polymer 52 2011 1490 1494
    • (2011) Polymer , vol.52 , pp. 1490-1494
    • Liu, W.-C.1    Castro, J.V.2    Gilbert, R.G.3
  • 22
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • N. Mesecke, N. Terziyska, C. Kozany, F. Baumann, W. Neupert, and K. Hell A disulfide relay system in the intermembrane space of mitochondria that mediates protein import Cell 121 2005 1059 1069
    • (2005) Cell , vol.121 , pp. 1059-1069
    • Mesecke, N.1    Terziyska, N.2    Kozany, C.3    Baumann, F.4    Neupert, W.5    Hell, K.6
  • 23
    • 0001744778 scopus 로고    scopus 로고
    • Determination of the degree of branching in normal and amylopectin type potato starch with H-1-NMR spectroscopy-Improved resolution and two-dimensional spectroscopy
    • G.S. Nilsson, K.E. Bergquist, U. Nilsson, and L. Gorton Determination of the degree of branching in normal and amylopectin type potato starch with H-1-NMR spectroscopy-Improved resolution and two-dimensional spectroscopy Starch 48 1996
    • (1996) Starch , vol.48
    • Nilsson, G.S.1    Bergquist, K.E.2    Nilsson, U.3    Gorton, L.4
  • 25
    • 61649113784 scopus 로고    scopus 로고
    • The unique branching patterns of deinococcus glycogen branching enzymes are determined by their N-terminal domains
    • M. Palomo, S. Kralj, M.J.E.C. van der Maarel, and L. Dijkhuizen The unique branching patterns of deinococcus glycogen branching enzymes are determined by their N-terminal domains Applied and Environmental Microbiology 75 2009 1355 1362
    • (2009) Applied and Environmental Microbiology , vol.75 , pp. 1355-1362
    • Palomo, M.1    Kralj, S.2    Van Der Maarel, M.J.E.C.3    Dijkhuizen, L.4
  • 27
    • 0035882732 scopus 로고    scopus 로고
    • Characterization of branched polymers by size exclusion chromatography coupled with multiangle light scattering detector. I. Size exclusion chromatography elution behavior of branched polymers
    • S. Podzimek, T. Vlcek, and C. Johann Characterization of branched polymers by size exclusion chromatography coupled with multiangle light scattering detector. I. Size exclusion chromatography elution behavior of branched polymers Journal of Applied Polymer Science 81 2001 1588 1594
    • (2001) Journal of Applied Polymer Science , vol.81 , pp. 1588-1594
    • Podzimek, S.1    Vlcek, T.2    Johann, C.3
  • 29
    • 0026219265 scopus 로고
    • Determination of kinetic parameters for maltotriose and higher malto oligosaccharides in the reactions catalyzed by α-d-glucan phosphorylase from potato
    • T. Suganuma, J.I. Kitazono, K. Yoshinaga, S. Fujimoto, and T. Nagahama Determination of kinetic parameters for maltotriose and higher malto oligosaccharides in the reactions catalyzed by α-d-glucan phosphorylase from potato Carbohydrate Research 217 1991 213 220
    • (1991) Carbohydrate Research , vol.217 , pp. 213-220
    • Suganuma, T.1    Kitazono, J.I.2    Yoshinaga, K.3    Fujimoto, S.4    Nagahama, T.5
  • 32
    • 78649663458 scopus 로고    scopus 로고
    • Characterization of branched polysaccharides using multiple-detection size separation techniques
    • F. Viliaplana, and R.G. Gilbert Characterization of branched polysaccharides using multiple-detection size separation techniques Journal of Separation Science 33 2010 3537 3554
    • (2010) Journal of Separation Science , vol.33 , pp. 3537-3554
    • Viliaplana, F.1    Gilbert, R.G.2
  • 34
    • 1642353442 scopus 로고    scopus 로고
    • Kinetic and substrate binding analysis of phosphorylase b via electrospray ionization mass spectrometry: A model for chemical proteomics of sugar phosphorylases
    • C.J. Zea, and N.L. Pohl Kinetic and substrate binding analysis of phosphorylase b via electrospray ionization mass spectrometry: A model for chemical proteomics of sugar phosphorylases Analytical Biochemistry 327 2004 107 113
    • (2004) Analytical Biochemistry , vol.327 , pp. 107-113
    • Zea, C.J.1    Pohl, N.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.