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Volumn 53, Issue 14, 2005, Pages 5708-5715

The identification of starch phosphorylase in the developing mungbean (Vigna radiata L.)

Author keywords

Activity staining; Mungbean; Native PAGE; Pho; SP; Starch phosphorylase; Vigna radiata

Indexed keywords

PEPTIDE FRAGMENT; STARCH PHOSPHORYLASE;

EID: 22544472427     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf050193f     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 33044502812 scopus 로고    scopus 로고
    • The discovery of starch biosynthesis
    • Kung, S.-D., Yang, S.-F., Eds.; World Scientific Publishing: London, England, Chapter 10
    • Preiss, J.; Sivak, M. N. The discovery of starch biosynthesis. In Discoveries in plant biology, 1st ed.; Kung, S.-D., Yang, S.-F., Eds.; World Scientific Publishing: London, England, 1998; Vol. III, Chapter 10, pp 217-237.
    • (1998) Discoveries in Plant Biology, 1st Ed. , vol.3 , pp. 217-237
    • Preiss, J.1    Sivak, M.N.2
  • 2
    • 0001328421 scopus 로고
    • The reversible formation of starch glucose 1-phosphate catalyzed by potato phosphorylase
    • Hanes, C. S. The reversible formation of starch glucose 1-phosphate catalyzed by potato phosphorylase. Proc. R. Soc. London, Ser. B. 1940, 129, 174-208.
    • (1940) Proc. R. Soc. London, Ser. B. , vol.129 , pp. 174-208
    • Hanes, C.S.1
  • 5
    • 0001549597 scopus 로고
    • Phosphorylase I and II of maize endosperm
    • Tsai, C. Y.; Nelson, O. E. Phosphorylase I and II of maize endosperm. Plant Physiol. 1968, 43, 103-112.
    • (1968) Plant Physiol. , vol.43 , pp. 103-112
    • Tsai, C.Y.1    Nelson, O.E.2
  • 6
    • 0016791221 scopus 로고
    • Maize α-glucan phosphorylase
    • Burr, B.; Nelson, O. E. Maize α-glucan phosphorylase. Eur. J. Biochem. 1975, 56, 539-546.
    • (1975) Eur. J. Biochem. , vol.56 , pp. 539-546
    • Burr, B.1    Nelson, O.E.2
  • 7
    • 0035298435 scopus 로고    scopus 로고
    • Purification and characterization of the maize amyloplast stromal 112-kDa starch phosphorylase
    • Mu, H. H.; Yu, Y.; Wasserman, B. P.; Carman, G. M. Purification and characterization of the maize amyloplast stromal 112-kDa starch phosphorylase. Arch. Biochem. Biophys. 2001, 388, 155-164.
    • (2001) Arch. Biochem. Biophys. , vol.388 , pp. 155-164
    • Mu, H.H.1    Yu, Y.2    Wasserman, B.P.3    Carman, G.M.4
  • 8
    • 0035141049 scopus 로고    scopus 로고
    • Identification of the maize amyloplast stromal 112-kDa protein as a plastidic starch phosphorylase
    • Yu, Y.; Mu, H. H.; Wasserman, B. P.; Carman, G. M. Identification of the maize amyloplast stromal 112-kDa protein as a plastidic starch phosphorylase. Plant Physiol. 2001, 125, 351-359.
    • (2001) Plant Physiol. , vol.125 , pp. 351-359
    • Yu, Y.1    Mu, H.H.2    Wasserman, B.P.3    Carman, G.M.4
  • 9
    • 5244329367 scopus 로고
    • Starch phosphorylase enzymes in developing and germinating pea seeds
    • Matheson, N. K.; Richardson, R. H. Starch phosphorylase enzymes in developing and germinating pea seeds. Phytochemistry 1976, 15, 887-892.
    • (1976) Phytochemistry , vol.15 , pp. 887-892
    • Matheson, N.K.1    Richardson, R.H.2
  • 10
    • 0041893776 scopus 로고
    • Intracellular localization of phosphorylases in spinach and pea leaves
    • Steup, M.; Latzko, E. Intracellular localization of phosphorylases in spinach and pea leaves. Planta 1979, 145, 69-75.
    • (1979) Planta , vol.145 , pp. 69-75
    • Steup, M.1    Latzko, E.2
  • 11
    • 0022464896 scopus 로고
    • Cytochemical location and biochemical analysis of the starch phosphorylase enzyme in pea seeds (Pisum sativum L. cv. Rivalin)
    • Vivo, A.; Felipe, M. R. Cytochemical location and biochemical analysis of the starch phosphorylase enzyme in pea seeds (Pisum sativum L. cv. Rivalin). Cell Mol. Biol. 1986, 32, 471-476.
    • (1986) Cell Mol. Biol. , vol.32 , pp. 471-476
    • Vivo, A.1    Felipe, M.R.2
  • 12
    • 0036885625 scopus 로고    scopus 로고
    • Activity and expression of banana starch phosphorylase during fruit development and ripening
    • Da Mota, R. V.; Cordenunsi, B. R.; do Nascimento, E.; Purgatto, E.; Rosseto, M. R.; Lajalo, F. M. Activity and expression of banana starch phosphorylase during fruit development and ripening. Planta 2002, 215, 325-333.
    • (2002) Planta , vol.215 , pp. 325-333
    • Da Mota, R.V.1    Cordenunsi, B.R.2    Do Nascimento, E.3    Purgatto, E.4    Rosseto, M.R.5    Lajalo, F.M.6
  • 13
    • 0020485869 scopus 로고
    • Purification and physicochemical properties of starch phosphorylase from young banana leaves
    • Kumar, A.; Sanwal, G. G. Purification and physicochemical properties of starch phosphorylase from young banana leaves. Biochemistry 1982, 21, 4152-4159.
    • (1982) Biochemistry , vol.21 , pp. 4152-4159
    • Kumar, A.1    Sanwal, G.G.2
  • 14
    • 0344733004 scopus 로고
    • α-1,4-Glucan phosphorylase forms from leaves of spinach (Spinacia oleracea L.). I. In situ localization by indirect immunofluorescence
    • Schachtele, C.; Steup, M. α-1,4-Glucan phosphorylase forms from leaves of spinach (Spinacia oleracea L.). I. In situ localization by indirect immunofluorescence. Planta 1986, 167, 444-451.
    • (1986) Planta , vol.167 , pp. 444-451
    • Schachtele, C.1    Steup, M.2
  • 15
    • 0023023420 scopus 로고
    • The complete amino acid sequence of potato α-glucan phosphorylase
    • Nakano, K.; Fukui, T. The complete amino acid sequence of potato α-glucan phosphorylase. J. Biol. Chem. 1986, 261, 8230-8236.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8230-8236
    • Nakano, K.1    Fukui, T.2
  • 16
    • 0023406749 scopus 로고
    • Two types of phosphorylases from etiolated soybean
    • Suda, M.; Watanabe, T.; Kobayashi, M.; Matsuda, K. Two types of phosphorylases from etiolated soybean. J. Biochem. 1987, 102, 471-479.
    • (1987) J. Biochem. , vol.102 , pp. 471-479
    • Suda, M.1    Watanabe, T.2    Kobayashi, M.3    Matsuda, K.4
  • 17
    • 0008897574 scopus 로고
    • Sweet potato starch phosphorylase-purification and characterization
    • Chang, T.-C; Lee, P.-D.; Su, J.-C. Sweet potato starch phosphorylase-purification and characterization. Agric. Biol. Chem. 1987, 51, 187-195.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 187-195
    • Chang, T.-C.1    Lee, P.-D.2    Su, J.-C.3
  • 18
    • 0000574302 scopus 로고
    • Primary structure of sweet potato starch phosphorylase deduced from its cDNA sequence
    • Lin, C.-T.; Yeh, K.-W.; Lee, P.-D.; Su, J.-C. Primary structure of sweet potato starch phosphorylase deduced from its cDNA sequence. Plant Physiol. 1991, 95, 1250-1253.
    • (1991) Plant Physiol. , vol.95 , pp. 1250-1253
    • Lin, C.-T.1    Yeh, K.-W.2    Lee, P.-D.3    Su, J.-C.4
  • 19
    • 0008923759 scopus 로고
    • Native and degraded forms of sweet potato starch phosphorylase
    • Chiang, C. L.; Lu, Y. L.; Juang, R. H.; Lee, P. D.; Su, J. C. Native and degraded forms of sweet potato starch phosphorylase. Agric. Biol. Chem. 1991, 55, 641-646.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 641-646
    • Chiang, C.L.1    Lu, Y.L.2    Juang, R.H.3    Lee, P.D.4    Su, J.C.5
  • 20
    • 0036239415 scopus 로고    scopus 로고
    • Regulation of the catalytic behaviour of L-form starch phosphorylase from sweet potato roots by proteolysis
    • Chen, H. M.; Chang, S. C.; Wu, C. C.; Cuo, T. S.; Wu, J. S.; Juang, R. H. Regulation of the catalytic behaviour of L-form starch phosphorylase from sweet potato roots by proteolysis. Physiol. Plant. 2002, 114, 506-515.
    • (2002) Physiol. Plant. , vol.114 , pp. 506-515
    • Chen, H.M.1    Chang, S.C.2    Wu, C.C.3    Cuo, T.S.4    Wu, J.S.5    Juang, R.H.6
  • 21
    • 0030057260 scopus 로고    scopus 로고
    • Multiple forms of starch phosphorylase from sorghum leaves
    • Venkaiah, B.; Kumar, A. Multiple forms of starch phosphorylase from sorghum leaves. Phytochemistry 1996, 41, 713-717.
    • (1996) Phytochemistry , vol.41 , pp. 713-717
    • Venkaiah, B.1    Kumar, A.2
  • 22
    • 0029691899 scopus 로고    scopus 로고
    • Glucan phosphorylases in Vicia faba L.: Cloning, structural analysis and expression patterns of cytosolic and plastidic forms in relation to starch
    • Buchner, P.; Borisjuk, L.; Wobus, U. Glucan phosphorylases in Vicia faba L.: cloning, structural analysis and expression patterns of cytosolic and plastidic forms in relation to starch. Planta 1996, 199, 64-73.
    • (1996) Planta , vol.199 , pp. 64-73
    • Buchner, P.1    Borisjuk, L.2    Wobus, U.3
  • 23
    • 4143136472 scopus 로고    scopus 로고
    • Purification and characterization of a cytosolic starch phosphorylase from etiolated rice seedlings
    • Hsu, J.-H.; Yang, C.-C; Su, J.-C.; Lee, P.-D. Purification and characterization of a cytosolic starch phosphorylase from etiolated rice seedlings. Bot. Bull. Acad. Sin. 2004, 45, 187-196.
    • (2004) Bot. Bull. Acad. Sin. , vol.45 , pp. 187-196
    • Hsu, J.-H.1    Yang, C.-C.2    Su, J.-C.3    Lee, P.-D.4
  • 24
    • 0014500018 scopus 로고
    • Kinetic mechanism of maltodextrin phosphorylase
    • Chao, J.; Johnson, G. F.; Graves, D. J. Kinetic mechanism of maltodextrin phosphorylase. Biochemistry 1969, 8, 1459-1466.
    • (1969) Biochemistry , vol.8 , pp. 1459-1466
    • Chao, J.1    Johnson, G.F.2    Graves, D.J.3
  • 25
    • 0027414321 scopus 로고
    • A chimeric α-glucan phosphorylase of plant type L and H isozymes
    • Mori, H.; Tanizawa, K.; Fukui, T. A chimeric α-glucan phosphorylase of plant type L and H isozymes. J. Biol. Chem. 1993, 268, 5574-5581.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5574-5581
    • Mori, H.1    Tanizawa, K.2    Fukui, T.3
  • 26
    • 0018788558 scopus 로고
    • Some properties of starch phosphorylase from cotyledons of germinating seeds of Voandzeia subterranea
    • Umezurike, G. M.; Ekhorutomwen, S. A. Some properties of starch phosphorylase from cotyledons of germinating seeds of Voandzeia subterranea. Biochim. Biophys. Acta 1979, 567, 331-338.
    • (1979) Biochim. Biophys. Acta , vol.567 , pp. 331-338
    • Umezurike, G.M.1    Ekhorutomwen, S.A.2
  • 27
    • 21944439385 scopus 로고    scopus 로고
    • Physicochemical characterization of mung bean starch
    • Hoover, R.; Li, Y. X.; Hynes, G.; Senanayake, N. Physicochemical characterization of mung bean starch. Food Hydrocolloids 1997, 11, 401-408.
    • (1997) Food Hydrocolloids , vol.11 , pp. 401-408
    • Hoover, R.1    Li, Y.X.2    Hynes, G.3    Senanayake, N.4
  • 28
    • 33044483677 scopus 로고
    • Chemical analysis of mungbean seeds
    • Asia Vegetable Research and Development Center: Shanhua, Taiwan
    • AVRDC. Chemical analysis of mungbean seeds. Progress report; Asia Vegetable Research and Development Center: Shanhua, Taiwan, 1975.
    • (1975) Progress Report
  • 29
    • 21644449501 scopus 로고
    • Enzymes involves in starch synthesis in the developing mung bean seed
    • Tsay, J. S.; Kou, W. L.; Kuo. C. G. Enzymes involves in starch synthesis in the developing mung bean seed. Phytochemistry 1983, 22, 1573-1576.
    • (1983) Phytochemistry , vol.22 , pp. 1573-1576
    • Tsay, J.S.1    Kou, W.L.2    Kuo, C.G.3
  • 30
    • 33044494148 scopus 로고    scopus 로고
    • GBSS activities on mungbean (Vigna radiata L.) starch granule and analysis of its total protein profiles
    • Ko, Y.-T.; Chang, S.-K.; Chen, H.-C.; Li, Y.-C. GBSS activities on mungbean (Vigna radiata L.) starch granule and analysis of its total protein profiles. Taiwanese J. Agric. Chem. Food Sci. 2004, 42, 132-139.
    • (2004) Taiwanese J. Agric. Chem. Food Sci. , vol.42 , pp. 132-139
    • Ko, Y.-T.1    Chang, S.-K.2    Chen, H.-C.3    Li, Y.-C.4
  • 31
    • 33044489030 scopus 로고    scopus 로고
    • Mungbean (Vigna radiate L.) starch branching enzyme activity-related proteins in SDS-PAGE gel after renaturation
    • Ko, Y.-T.; Huang, L.-H. Mungbean (Vigna radiate L.) starch branching enzyme activity-related proteins in SDS-PAGE gel after renaturation. Taiwanese J. Agric. Chem. Food Sci. 2004, 42, 215-223.
    • (2004) Taiwanese J. Agric. Chem. Food Sci. , vol.42 , pp. 215-223
    • Ko, Y.-T.1    Huang, L.-H.2
  • 32
    • 21644433680 scopus 로고    scopus 로고
    • Detection of proteins related to starch synthase activity in the developing mungbean (Vigna radiata L.)
    • Ko, Y.-T.; Pan, C.-H.; Lee, Y.-T.; Chang, J.-Y. Detection of proteins related to starch synthase activity in the developing mungbean (Vigna radiata L.). J. Agric. Food Chem. 2005, 53, 4805-4812.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 4805-4812
    • Ko, Y.-T.1    Pan, C.-H.2    Lee, Y.-T.3    Chang, J.-Y.4
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0031571138 scopus 로고    scopus 로고
    • Sequencing of N-linked oligosaccharides directly from protein gels: In-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography
    • Kuster, B.; Wheeler, S. F.; Hunter, A. P.; Dwek, R. A.; Harvey, D. J. Sequencing of N-linked oligosaccharides directly from protein gels: In-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography. Anal. Biochem. 1997, 250, 82-101.
    • (1997) Anal. Biochem. , vol.250 , pp. 82-101
    • Kuster, B.1    Wheeler, S.F.2    Hunter, A.P.3    Dwek, R.A.4    Harvey, D.J.5
  • 35
    • 0034096536 scopus 로고    scopus 로고
    • Protein identification methods in proteomics
    • Gevaert, K.; Vandekerckhove, J. Protein identification methods in proteomics. Electrophoresis 2000, 21, 1145-1154.
    • (2000) Electrophoresis , vol.21 , pp. 1145-1154
    • Gevaert, K.1    Vandekerckhove, J.2
  • 36
    • 0033918391 scopus 로고    scopus 로고
    • Mass spectrometry: A tool for the identification of proteins separated by gels
    • Lahm, H.-W.; Langen, H. Mass spectrometry: a tool for the identification of proteins separated by gels. Electrophoresis 2000, 21, 2105-2114.
    • (2000) Electrophoresis , vol.21 , pp. 2105-2114
    • Lahm, H.-W.1    Langen, H.2


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