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Volumn 251, Issue 1-2, 1998, Pages 343-352

Homodimers and heterodimers of Pho1-type phosphorylase isoforms in Solanum tuberosum L. as revealed by sequence-specific antibodies

Author keywords

Heterodimer; Isoenzyme; Phosphorylase; Solanum tuberosum L; Starch metabolism

Indexed keywords

ENZYME ANTIBODY; ISOENZYME; PHOSPHORYLASE;

EID: 0032518586     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2510343.x     Document Type: Article
Times cited : (43)

References (33)
  • 2
    • 0026482961 scopus 로고
    • Tracking conformational states in allosteric transitions of phosphorylase
    • Browner, M. F., Fauman, E. B. & Flettrick, R. J. (1992) Tracking conformational states in allosteric transitions of phosphorylase, Biochemistry 31, 11297-11304.
    • (1992) Biochemistry , vol.31 , pp. 11297-11304
    • Browner, M.F.1    Fauman, E.B.2    Flettrick, R.J.3
  • 4
    • 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. (1996) Glucan phosphorylases in Vicia faba L.: cloning, structural analysis and expression patterns of cytosolic and plastidic forms in relation to starch, Planta 199, 64-73.
    • (1996) Planta , vol.199 , pp. 64-73
    • Buchner, P.1    Borisjuk, L.2    Wobus, U.3
  • 5
    • 0342703145 scopus 로고
    • Non-chloroplast α-1,4-glucan phosphorylase from pea leaves: Characterization and in situ localization by indirect immunofluorescence
    • Conrads, J., van Berkel, J., Schächtele, C. & Steup, M. (1986) Non-chloroplast α-1,4-glucan phosphorylase from pea leaves: Characterization and in situ localization by indirect immunofluorescence, Biochim. Biophys. Acta 882, 452-463.
    • (1986) Biochim. Biophys. Acta , vol.882 , pp. 452-463
    • Conrads, J.1    Van Berkel, J.2    Schächtele, C.3    Steup, M.4
  • 6
    • 0031239040 scopus 로고    scopus 로고
    • Induction of genes encoding plastidic phosphorylase from spinach (Spinacia oleracea L.) and potato (Solanum tuberosum L.) by exogenously supplied carbohydrates in excised leaf discs
    • Duwenig, E., Steup, M. & Kossmann, J. (1997) Induction of genes encoding plastidic phosphorylase from spinach (Spinacia oleracea L.) and potato (Solanum tuberosum L.) by exogenously supplied carbohydrates in excised leaf discs, Planta 203, 111-120.
    • (1997) Planta , vol.203 , pp. 111-120
    • Duwenig, E.1    Steup, M.2    Kossmann, J.3
  • 7
    • 0022425448 scopus 로고
    • Fructose-1,6-bisphosphatase from Synechococcus leopoliensis. Substrate-dependent dimertetramer interconversion
    • Gerbling, K.-P., Steup, M. & Latzko, E. (1985) Fructose-1,6-bisphosphatase from Synechococcus leopoliensis. Substrate-dependent dimertetramer interconversion, Eur. J. Biochem. 147, 207-215.
    • (1985) Eur. J. Biochem. , vol.147 , pp. 207-215
    • Gerbling, K.-P.1    Steup, M.2    Latzko, E.3
  • 8
    • 49049145128 scopus 로고
    • Affinity electrophoresis
    • Horejsi, V. (1981) Affinity electrophoresis, Anal. Biochem. 112, 1-8.
    • (1981) Anal. Biochem. , vol.112 , pp. 1-8
    • Horejsi, V.1
  • 9
    • 0027145152 scopus 로고
    • Evolution of allosteric control in glycogen phosphorylase
    • Hudson, J. W., Golding, G. B. & Crerar, M. M. (1993) Evolution of allosteric control in glycogen phosphorylase, J. Mol. Biol. 234, 700-721.
    • (1993) J. Mol. Biol. , vol.234 , pp. 700-721
    • Hudson, J.W.1    Golding, G.B.2    Crerar, M.M.3
  • 10
    • 0029278930 scopus 로고
    • Characterization of the maize gene sugary 1, a determinant of starch composition in kernels
    • James, M. G., Robertson, D. R. & Myers, A. M. (1995) Characterization of the maize gene sugary 1, a determinant of starch composition in kernels, Plant Cell 7, 417-429.
    • (1995) Plant Cell , vol.7 , pp. 417-429
    • James, M.G.1    Robertson, D.R.2    Myers, A.M.3
  • 13
    • 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. (1990) Primary structure of sweet potato starch phosphorylase deduced from its cDNA sequence, Plant Physiol. 95, 1250-1253.
    • (1990) Plant Physiol. , vol.95 , pp. 1250-1253
    • Lin, C.T.1    Yeh, K.-W.2    Lee, P.-D.3    Su, J.-C.4
  • 14
    • 0023147728 scopus 로고
    • A simple, non-chromatographic procedure to purify immunglobulins from serum and ascites fluids
    • McKinney, M. M. & Parkinson, A. (1987) A simple, non-chromatographic procedure to purify immunglobulins from serum and ascites fluids, J. Immunol. Methods 96, 271-278.
    • (1987) J. Immunol. Methods , vol.96 , pp. 271-278
    • McKinney, M.M.1    Parkinson, A.2
  • 15
    • 0025955179 scopus 로고
    • Potato tuber type H phosphorylase isozyme
    • Mori, H., Tanizawa, K. & Fukui, T. (1991) Potato tuber type H phosphorylase isozyme, J. Biol. Chem. 266, 18 446-18 453.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18446-18453
    • Mori, H.1    Tanizawa, K.2    Fukui, T.3
  • 16
    • 0027435089 scopus 로고
    • Engineered plant phosphorylase showing extraordinarily high affinity for various α-glucan molecules
    • Mori, H., Tanizawa, K. & Fukui, T. (1993a) Engineered plant phosphorylase showing extraordinarily high affinity for various α-glucan molecules, Protein Sci. 2, 1621-1629.
    • (1993) Protein Sci. , vol.2 , pp. 1621-1629
    • Mori, H.1    Tanizawa, K.2    Fukui, T.3
  • 17
    • 0027414321 scopus 로고
    • A chimeric α-glucan phosphorylase of plant type L and H isozymes
    • Mori, H., Tanizawa, K. & Fukui, T. (1993b) A chimeric α-glucan phosphorylase of plant type L and H isozymes, J. Biol. Chem. 268, 5574-5581.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5574-5581
    • Mori, H.1    Tanizawa, K.2    Fukui, T.3
  • 19
    • 0023037669 scopus 로고
    • Amino acid sequence of cyanogen bromide fragments of potato
    • Nakano, K., Tashiro, Y. Kikumoto, Y., Tagaya, M. & Fukui, T. (1986) Amino acid sequence of cyanogen bromide fragments of potato, J. Biol. Chem. 261, 8224-8229.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8224-8229
    • Nakano, K.1    Tashiro, Y.2    Kikumoto, Y.3    Tagaya, M.4    Fukui, T.5
  • 20
    • 0023023420 scopus 로고
    • The complete amino acid sequence of potato α-glucan phosphorylase
    • Nakano, K. & Fukui, T. (1986) The complete amino acid sequence of potato α-glucan phosphorylase, J. Biol. Chem. 261, 8230-8236.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8230-8236
    • Nakano, K.1    Fukui, T.2
  • 22
    • 0023316642 scopus 로고
    • E. coli maltodextrin phosphorylase: Primare structure and deletion mapping of the C-terminal site
    • Palm, D., Goerl, R., Weidinger, G., Zeier, R., Fischer, B. & Schinzel, R. (1987) E. coli maltodextrin phosphorylase: primare structure and deletion mapping of the C-terminal site, Z. Naturforsch. 42c, 394-400.
    • (1987) Z. Naturforsch. , vol.42 C , pp. 394-400
    • Palm, D.1    Goerl, R.2    Weidinger, G.3    Zeier, R.4    Fischer, B.5    Schinzel, R.6
  • 25
    • 0344733004 scopus 로고
    • α-Glucan phosphorylase forms from leaves of spinach (Spinacia oleracea L.): I. in situ localization by indirect immunofluorescence
    • Schächtele, C. & Steup, M. (1986) α-Glucan phosphorylase forms from leaves of spinach (Spinacia oleracea L.): I. In situ localization by indirect immunofluorescence, Planta 167, 444-451.
    • (1986) Planta , vol.167 , pp. 444-451
    • Schächtele, C.1    Steup, M.2
  • 26
    • 0013959181 scopus 로고
    • Location of the maltose A and B loci on the genetic map of Escherichia coli
    • Schwartz, M. (1966) Location of the maltose A and B loci on the genetic map of Escherichia coli, J. Bacteriol. 92, 1083-1089.
    • (1966) J. Bacteriol. , vol.92 , pp. 1083-1089
    • Schwartz, M.1
  • 28
    • 0029240175 scopus 로고
    • A second L-type isozyme of potato glucan phosphorylase: Cloning, anti-sense inhibition and expression analysis
    • Sonnewald, U., Basner, A., Greve, B. & Steup, M. (1995) A second L-type isozyme of potato glucan phosphorylase: cloning, anti-sense inhibition and expression analysis, Plant Mol. Biol. 27, 567-576.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 567-576
    • Sonnewald, U.1    Basner, A.2    Greve, B.3    Steup, M.4
  • 29
    • 84940995250 scopus 로고
    • Starch degradation
    • (Preiss, J., ed.) Academic Press, New York
    • Steup, M. (1988) Starch degradation, in Biochemistry of plants, vol. 14, Carbohydrates (Preiss, J., ed.) pp. 255-296, Academic Press, New York.
    • (1988) Biochemistry of Plants, Vol. 14, Carbohydrates , vol.14 , pp. 255-296
    • Steup, M.1
  • 30
    • 0003203125 scopus 로고
    • Starch degrading enzymes
    • (Lea, P. J., ed.) Academic Press, New York
    • Steup, M. (1990) Starch degrading enzymes, in Methods in plant biochemistry, vol. 3 (Lea, P. J., ed.) pp. 103-131, Academic Press, New York.
    • (1990) Methods in Plant Biochemistry , vol.3 , pp. 103-131
    • Steup, M.1
  • 31
    • 84988123054 scopus 로고
    • Affinity electrophoresis: Principles and applications
    • Takeo, K. (1984) Affinity electrophoresis: principles and applications, Electrophoresis 5, 187-195.
    • (1984) Electrophoresis , vol.5 , pp. 187-195
    • Takeo, K.1
  • 33
    • 0000554896 scopus 로고
    • Glucan-phosphorylase forms in cotyledons of Pisum sativum L.: Localization, developmental change, in vitro translation and processing
    • van Berkel, J., Conrads-Strauch, J. & Steup, M. (1991) Glucan-phosphorylase forms in cotyledons of Pisum sativum L.: localization, developmental change, in vitro translation and processing, Planta 185, 432-439.
    • (1991) Planta , vol.185 , pp. 432-439
    • Van Berkel, J.1    Conrads-Strauch, J.2    Steup, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.