메뉴 건너뛰기




Volumn 324, Issue 1, 2004, Pages 52-59

An assay for adenosine 5′-diphosphate (ADP)-glucose pyrophosphorylase that measures the synthesis of radioactive ADP-glucose with glycogen synthase

Author keywords

ADP glucose; ADP glucose pyrophosphorylase; Glycogen synthase; Polysaccharide precipitation

Indexed keywords

ESCHERICHIA COLI; RADIATION; RADIOACTIVITY;

EID: 0344494024     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2003.09.024     Document Type: Article
Times cited : (21)

References (34)
  • 1
    • 0001395823 scopus 로고
    • Bacterial glycogen and plant starch biosynthesis
    • Iglesias A.A., Preiss J. Bacterial glycogen and plant starch biosynthesis. Biochem. Educ. 20:1992;196-203.
    • (1992) Biochem. Educ. , vol.20 , pp. 196-203
    • Iglesias, A.A.1    Preiss, J.2
  • 2
    • 0001261938 scopus 로고
    • Enzymic synthesis of adenosine diphosphate glucose from glucose-1-phosphate and adenosine triphosphate
    • Espada J. Enzymic synthesis of adenosine diphosphate glucose from glucose-1-phosphate and adenosine triphosphate. J. Biol. Chem. 237:1962;3577-3581.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3577-3581
    • Espada, J.1
  • 3
    • 0031613064 scopus 로고    scopus 로고
    • Biochemistry, molecular biology and regulation of starch synthesis
    • Preiss J., Sivak M.N. Biochemistry, molecular biology and regulation of starch synthesis. Genet. Eng. 20:1998;177-223.
    • (1998) Genet. Eng. , vol.20 , pp. 177-223
    • Preiss, J.1    Sivak, M.N.2
  • 4
    • 0038653402 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis
    • Ballicora M.A., Iglesias A.A., Preiss J. ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis. Microbiol. Mol. Biol. Rev. 67:2003;213-225.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 213-225
    • Ballicora, M.A.1    Iglesias, A.A.2    Preiss, J.3
  • 5
    • 0021144092 scopus 로고
    • Bacterial glycogen synthesis and its regulation
    • Preiss J. Bacterial glycogen synthesis and its regulation. Annu. Rev. Microbiol. 38:1984;419-458.
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 419-458
    • Preiss, J.1
  • 6
    • 0345566505 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase; a regulatory enzyme for plant starch synthesis
    • in press
    • Ballicora MA, Iglesias A, Preiss J, ADP-glucose pyrophosphorylase; a regulatory enzyme for plant starch synthesis, Photosynth. Res. (2003) in press.
    • (2003) Photosynth. Res.
    • Ballicora, M.A.1    Iglesias, A.2    Preiss, J.3
  • 7
    • 0037327287 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase from potato tuber: Site-directed mutagenesis of homologous aspartic acid residues in the small and large subunits
    • Frueauf J.B., Ballicora M.A., Preiss J. ADP-glucose pyrophosphorylase from potato tuber: site-directed mutagenesis of homologous aspartic acid residues in the small and large subunits. Plant J. 33:2003;503-511.
    • (2003) Plant J. , vol.33 , pp. 503-511
    • Frueauf, J.B.1    Ballicora, M.A.2    Preiss, J.3
  • 9
    • 0037199461 scopus 로고    scopus 로고
    • Characterization of chimeric ADP-glucose pyrophosphorylases of Escherichia coli and Agrobacterium tumefaciens. Importance of the C- terminus on the selectivity for allosteric regulators
    • Ballicora M.A., Sesma J.I., Iglesias A.A., Preiss J. Characterization of chimeric ADP-glucose pyrophosphorylases of Escherichia coli and Agrobacterium tumefaciens. Importance of the C- terminus on the selectivity for allosteric regulators. Biochemistry. 41:2002;9431-9437.
    • (2002) Biochemistry , vol.41 , pp. 9431-9437
    • Ballicora, M.A.1    Sesma, J.I.2    Iglesias, A.A.3    Preiss, J.4
  • 10
    • 0000857965 scopus 로고
    • The activation and inhibition of bacterial adenosine-diphosphoglucose pyrophosphorylase
    • Shen L., Preiss J. The activation and inhibition of bacterial adenosine-diphosphoglucose pyrophosphorylase. Biochem. Biophys. Res. Commun. 17:1964;424-429.
    • (1964) Biochem. Biophys. Res. Commun. , vol.17 , pp. 424-429
    • Shen, L.1    Preiss, J.2
  • 11
    • 0014011424 scopus 로고
    • Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach leaf chloroplasts
    • Ghosh H.P., Preiss J. Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach leaf chloroplasts. J. Biol. Chem. 241:1966;4491-4504.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4491-4504
    • Ghosh, H.P.1    Preiss, J.2
  • 12
    • 0018898581 scopus 로고
    • A rapid, sensitive assay for starch phosphorylase and ADPglucose pyrophosphorylase
    • McCracken D.A., Rutherford W.M. A rapid, sensitive assay for starch phosphorylase and ADPglucose pyrophosphorylase. Anal. Biochem. 101:1980;275-277.
    • (1980) Anal. Biochem. , vol.101 , pp. 275-277
    • Mccracken, D.A.1    Rutherford, W.M.2
  • 13
    • 0019426975 scopus 로고
    • A rapid and sensitive assay of ADP-glucose pyrophosphorylase using luciferase
    • Ching T.M. A rapid and sensitive assay of ADP-glucose pyrophosphorylase using luciferase. Anal. Biochem. 111:1981;327-330.
    • (1981) Anal. Biochem. , vol.111 , pp. 327-330
    • Ching, T.M.1
  • 14
    • 0026458333 scopus 로고
    • Role of ADPglucose pyrophosphorylase in regulating starch levels in plant tissues
    • Stark D.M., Timmerman K.P., Barry G.F., Preiss J., Kishore G.M. Role of ADPglucose pyrophosphorylase in regulating starch levels in plant tissues. Science. 258:1992;287-292.
    • (1992) Science , vol.258 , pp. 287-292
    • Stark, D.M.1    Timmerman, K.P.2    Barry, G.F.3    Preiss, J.4    Kishore, G.M.5
  • 15
    • 0028893408 scopus 로고
    • A capillary zone electrophoresis assay for the nucleoside transfer enzyme adenosine diphosphate-glucose pyrophosphorylase
    • Roberts M.W., Preiss J., Okita T.W. A capillary zone electrophoresis assay for the nucleoside transfer enzyme adenosine diphosphate-glucose pyrophosphorylase. Anal. Biochem. 225:1995;121-126.
    • (1995) Anal. Biochem. , vol.225 , pp. 121-126
    • Roberts, M.W.1    Preiss, J.2    Okita, T.W.3
  • 16
    • 0001172247 scopus 로고
    • The rb mutation of peas causes structural and regulatory changes in ADP-Glc pyrophosphorylase from developing embryos
    • Hylton C., Smith A.M. The rb mutation of peas causes structural and regulatory changes in ADP-Glc pyrophosphorylase from developing embryos. Plant Physiol. 99:1992;1626-1634.
    • (1992) Plant Physiol. , vol.99 , pp. 1626-1634
    • Hylton, C.1    Smith, A.M.2
  • 17
    • 0344704348 scopus 로고
    • ADP-glucose pyrophosphorylase from corn grain
    • Espada J. ADP-glucose pyrophosphorylase from corn grain. Methods Enzymol. 8:1966;259-262.
    • (1966) Methods Enzymol. , vol.8 , pp. 259-262
    • Espada, J.1
  • 18
    • 0017231241 scopus 로고
    • Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B ADP-glucose:1,4-α-D-glucan 4-α- glucosyltransferase
    • Fox J., Kawaguchi K., Greenberg E., Preiss J. Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B ADP-glucose:1,4-α-D-glucan 4-α-glucosyltransferase. Biochemistry. 15:1976;849-857.
    • (1976) Biochemistry , vol.15 , pp. 849-857
    • Fox, J.1    Kawaguchi, K.2    Greenberg, E.3    Preiss, J.4
  • 20
    • 0035824612 scopus 로고    scopus 로고
    • Aspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli
    • Frueauf J.B., Ballicora M.A., Preiss J. Aspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli. J. Biol. Chem. 276:2001;46319-46325.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46319-46325
    • Frueauf, J.B.1    Ballicora, M.A.2    Preiss, J.3
  • 21
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves
    • Hill A.V. The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves. J. Physiol. (Lond.). 40:1910;4-7.
    • (1910) J. Physiol. (Lond.) , vol.40 , pp. 4-7
    • Hill, A.V.1
  • 23
    • 0343958760 scopus 로고
    • The ocurrence of adenosine diphosphate glucose: Glycogen transglucosylase in bacteria
    • Greenberg E., Preiss J. The ocurrence of adenosine diphosphate glucose: glycogen transglucosylase in bacteria. J. Biol. Chem. 239:1964;PC4314-4315.
    • (1964) J. Biol. Chem. , vol.239 , pp. 4314-4315
    • Greenberg, E.1    Preiss, J.2
  • 24
    • 0002339947 scopus 로고
    • Isolation and fractionation of polysaccharides
    • G.O. Aspinall. New York: Academic Press
    • Aspinall G.O. Isolation and fractionation of polysaccharides. Aspinall G.O. The Polysaccharides. 1982;19-34 Academic Press, New York.
    • (1982) The Polysaccharides , pp. 19-34
    • Aspinall, G.O.1
  • 25
    • 0014226072 scopus 로고
    • Regulation of muscle glycogen synthetase by metabolites. Differential effects on the I and D forms
    • Piras R., Rothman L.B., Cabib E. Regulation of muscle glycogen synthetase by metabolites. Differential effects on the I and D forms. Biochemistry. 7:1968;56-66.
    • (1968) Biochemistry , vol.7 , pp. 56-66
    • Piras, R.1    Rothman, L.B.2    Cabib, E.3
  • 26
    • 0014114022 scopus 로고
    • The stimulation of glycogen synthesis and of glycogen synthetase in the liver by the administration of glucose
    • De Wulf H., Hers H.G. The stimulation of glycogen synthesis and of glycogen synthetase in the liver by the administration of glucose. Eur. J. Biochem. 2:1967;50-56.
    • (1967) Eur. J. Biochem. , vol.2 , pp. 50-56
    • De Wulf, H.1    Hers, H.G.2
  • 27
  • 28
    • 0011916399 scopus 로고
    • Comparison of the glycogens isolated by acid and alkaline procedures
    • Stetten M.R., Katzen H.M., Stetten D. Comparison of the glycogens isolated by acid and alkaline procedures. J. Biol. Chem. 232:1958;475.
    • (1958) J. Biol. Chem. , vol.232 , pp. 475
    • Stetten, M.R.1    Katzen, H.M.2    Stetten, D.3
  • 29
    • 0037404135 scopus 로고    scopus 로고
    • Frog oocyte glycogen synthase: Enzyme regulation under in vitro and in vivo conditions
    • Báez M., Preller A., Ureta T. Frog oocyte glycogen synthase: enzyme regulation under in vitro and in vivo conditions. Arch. Biochem. Biophys. 413:2003;9-16.
    • (2003) Arch. Biochem. Biophys. , vol.413 , pp. 9-16
    • Báez, M.1    Preller, A.2    Ureta, T.3
  • 31
    • 0015983293 scopus 로고
    • Interaction of spinach leaf adenosine-diphosphate glucose α-1,4-glucan α-4-glucosyl transferase and α-1,4-glucan, α-1,4-glucan-6-glycosyl transferase in synthesis of branched α-glucan
    • Hawker J.S., Ozbun J.L., Ozaki H., Greenber E., Preiss J. Interaction of spinach leaf adenosine-diphosphate glucose α-1,4-glucan α-4-glucosyl transferase and α-1,4-glucan, α-1,4-glucan-6- glycosyl transferase in synthesis of branched α-glucan. Arch. Biochem. Biophys. 160:1974;530-551.
    • (1974) Arch. Biochem. Biophys. , vol.160 , pp. 530-551
    • Hawker, J.S.1    Ozbun, J.L.2    Ozaki, H.3    Greenber, E.4    Preiss, J.5
  • 32
    • 0345134941 scopus 로고
    • Radiometric assays
    • R. Eisenthal, & M.J. Danson. Oxford, New York, Tokyo: IRL press
    • Oldham K.G. Radiometric assays. Eisenthal R., Danson M.J. Enzyme Assays. A Practical Approach. 1992;93-122 IRL press, Oxford, New York, Tokyo.
    • (1992) Enzyme Assays. A Practical Approach , pp. 93-122
    • Oldham, K.G.1
  • 34
    • 0015149465 scopus 로고
    • Problems in the radiometric assessment of protein and nucleic acid synthesis
    • Oldham K.G. Problems in the radiometric assessment of protein and nucleic acid synthesis. Anal. Biochem. 44:1971;143-153.
    • (1971) Anal. Biochem. , vol.44 , pp. 143-153
    • Oldham, K.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.