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Volumn 13, Issue 3, 1998, Pages 419-425

cDNA cloning and characterisation of an α-glucosidase gene from potato (Solanum tuberosum L.)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GLUCOSIDASE; COMPLEMENTARY DNA; MALTOSE; PLANT DNA;

EID: 0032005953     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1998.00051.x     Document Type: Article
Times cited : (12)

References (40)
  • 1
    • 0027673057 scopus 로고
    • Isolation and analysis of a cDNA clone encoding the small subunit of ADP-glucose pyrophosphorylase from wheat
    • Ainsworth, C., Tarvis, M. and Clark, J. (1993) Isolation and analysis of a cDNA clone encoding the small subunit of ADP-glucose pyrophosphorylase from wheat. Plant Mol. Biol. 23, 23-33.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 23-33
    • Ainsworth, C.1    Tarvis, M.2    Clark, J.3
  • 2
    • 0003114654 scopus 로고
    • Biosynthesis and degradation of starch in higher plants
    • Beck, E. and Ziegler, P. (1989) Biosynthesis and degradation of starch in higher plants. In Ann. Rev. Plant Phys. & Mol. Biol. 40, 95-117.
    • (1989) Ann. Rev. Plant Phys. & Mol. Biol. , vol.40 , pp. 95-117
    • Beck, E.1    Ziegler, P.2
  • 3
    • 0003341874 scopus 로고
    • Partial characterization and subcellular location of three α-glucosidase isoforms in pea (Pisum sativum L.) seedlings
    • Beers, E.P., Duke, S.H. and Henson, C.A. (1990) Partial characterization and subcellular location of three α-glucosidase isoforms in pea (Pisum sativum L.) seedlings. Plant Physiol. 94, 738-744.
    • (1990) Plant Physiol. , vol.94 , pp. 738-744
    • Beers, E.P.1    Duke, S.H.2    Henson, C.A.3
  • 4
    • 0001719907 scopus 로고
    • Hydrolytic enzymes in the central vacuole of plant cells
    • Bolle, T. and Kende, H. (1979) Hydrolytic enzymes in the central vacuole of plant cells. Plant Physiol. 63, 1123-1132.
    • (1979) Plant Physiol. , vol.63 , pp. 1123-1132
    • Bolle, T.1    Kende, H.2
  • 5
    • 60849113198 scopus 로고
    • Plant α-glucosidases
    • Amylase Research Society of Japan, ed.. New York: Permagon Press
    • Chiba, S. (1988) Plant α-glucosidases. In Handbook of Amylases and Related Enzymes (Amylase Research Society of Japan, ed.). New York: Permagon Press, pp. 109-112.
    • (1988) Handbook of Amylases and Related Enzymes , pp. 109-112
    • Chiba, S.1
  • 6
    • 84954946456 scopus 로고
    • Purification and some properties of flint corn α-glucosidase
    • Chiba, S. and Shimomura, T. (1975) Purification and some properties of flint corn α-glucosidase. Agric. Biol. Chem. 39, 1041-1047.
    • (1975) Agric. Biol. Chem. , vol.39 , pp. 1041-1047
    • Chiba, S.1    Shimomura, T.2
  • 7
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. (1986) A new method for predicting signal sequence cleavage sites. Nucl Acid Res. 14, 4683-4690.
    • (1986) Nucl Acid Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 8
    • 0027225980 scopus 로고
    • New families in the classification of glucosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and Bairoch, A. (1993) New families in the classification of glucosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293, 781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 9
    • 0024026526 scopus 로고
    • Primary structure and processing of lysosomal alpha-glucosidase: Homology with the intestinal sucrase-isomaltase complex
    • Hoefsloot, L.H., Hoogeveen-Westerveld, M., Kroos, M.A., van Beeumen, J., Reuser, A.J.J. and Oostra, B.A. (1988) Primary structure and processing of lysosomal alpha-glucosidase: homology with the intestinal sucrase-isomaltase complex. EMBO J. 7, 1697-1704.
    • (1988) EMBO J. , vol.7 , pp. 1697-1704
    • Hoefsloot, L.H.1    Hoogeveen-Westerveld, M.2    Kroos, M.A.3    Van Beeumen, J.4    Reuser, A.J.J.5    Oostra, B.A.6
  • 10
    • 0022504432 scopus 로고
    • The sucrase-isomaltase complex: Primary structure, membrane orientation and evolution of a stalked intrinsic brush border protein
    • Hunziker, W., Spiess, M., Semenza, G. and Lodish, H.F. (1986) The sucrase-isomaltase complex: primary structure, membrane orientation and evolution of a stalked intrinsic brush border protein. Cell, 46, 227-234.
    • (1986) Cell , vol.46 , pp. 227-234
    • Hunziker, W.1    Spiess, M.2    Semenza, G.3    Lodish, H.F.4
  • 11
    • 0021471049 scopus 로고
    • Sequences that regulate the divergent GAL1-Gal10 promoter in Saccharomyces cerevisiae
    • Johnston, M. and Davis, R.W. (1984) Sequences that regulate the divergent GAL1-Gal10 promoter in Saccharomyces cerevisiae. Mol. Cell Biol. 4, 1440-1448.
    • (1984) Mol. Cell Biol. , vol.4 , pp. 1440-1448
    • Johnston, M.1    Davis, R.W.2
  • 12
    • 0343221074 scopus 로고
    • Improved method for purification of buckwheat α-glucosidase and some kinetic properties
    • Kanaya, K., Chiba, S., Shimomura, T. and Nishi, K (1976) Improved method for purification of buckwheat α-glucosidase and some kinetic properties. Agr. Biol. Chem. 40, 1929-1936.
    • (1976) Agr. Biol. Chem. , vol.40 , pp. 1929-1936
    • Kanaya, K.1    Chiba, S.2    Shimomura, T.3    Nishi, K.4
  • 13
    • 0001575206 scopus 로고
    • Properties of potato alpha-glucosidase
    • Killilea, S.D. and Clancy, M.J. (1978) Properties of potato alpha-glucosidase. Phytochemistry, 17, 1429-1431.
    • (1978) Phytochemistry , vol.17 , pp. 1429-1431
    • Killilea, S.D.1    Clancy, M.J.2
  • 14
    • 0026042790 scopus 로고
    • Primary structure and processing of the Candida tsukubaenis α-glucosidase. Homology with the rabbit intestinal sucraseisomaltase complex and human lysosomal α-glucosidase
    • Kinsella, T., Hogan, S., Larkin, A. and Cantwell, B.A. (1991) Primary structure and processing of the Candida tsukubaenis α-glucosidase. Homology with the rabbit intestinal sucraseisomaltase complex and human lysosomal α-glucosidase. Eur. J. Biochem. 202, 657-664.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 657-664
    • Kinsella, T.1    Hogan, S.2    Larkin, A.3    Cantwell, B.A.4
  • 15
    • 0010907005 scopus 로고
    • Partial purification and characterization of acid and neutral α-glucosidases from preclimacteric banana pulp tissues
    • Konishi, Y., Kitazato, S. and Nakatani, N. (1992) Partial purification and characterization of acid and neutral α-glucosidases from preclimacteric banana pulp tissues. Biosci. Biotech. Biochem. 56, 2046-2051.
    • (1992) Biosci. Biotech. Biochem. , vol.56 , pp. 2046-2051
    • Konishi, Y.1    Kitazato, S.2    Nakatani, N.3
  • 16
    • 0024487237 scopus 로고
    • Cloning and characterization of baker's yeast alpha-glucosidase: Over-expression in a yeast strain devoid of vacuolar proteinases
    • Kopetzki, E., Buckel, P. and Schumacher, G. (1989) Cloning and characterization of baker's yeast alpha-glucosidase: over-expression in a yeast strain devoid of vacuolar proteinases. Yeast, 5, 11-24.
    • (1989) Yeast , vol.5 , pp. 11-24
    • Kopetzki, E.1    Buckel, P.2    Schumacher, G.3
  • 17
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak, M. (1986) Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell, 44, 283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 18
    • 6844244157 scopus 로고
    • Starch
    • Day, P.M., ed.. New Tork: Academic Press
    • Manners, D.J. (1985) Starch. In Plant Carbohydrate Biochemistry (Day, P.M., ed.). New Tork: Academic Press, pp. 109-125.
    • (1985) Plant Carbohydrate Biochemistry , pp. 109-125
    • Manners, D.J.1
  • 19
    • 0028940690 scopus 로고
    • Analysis of carbohydrate transport across the envelope of isolated cauliflower-bud amyloplasts
    • Mohlmann, T., Batz, O., Maass, U. and Neuhaus, H.E. (1995) Analysis of carbohydrate transport across the envelope of isolated cauliflower-bud amyloplasts. Biochem. J. 307, 521-526.
    • (1995) Biochem. J. , vol.307 , pp. 521-526
    • Mohlmann, T.1    Batz, O.2    Maass, U.3    Neuhaus, H.E.4
  • 20
    • 0028674857 scopus 로고
    • Genes galore: A summary of methods for accessing results from large-scale partial sequencing of anonymous Arabidopsis cDNA clones
    • Newman, T., de Bruijn, F.J., Green, P. et al. (1994) Genes galore: a summary of methods for accessing results from large-scale partial sequencing of anonymous Arabidopsis cDNA clones. Plant Physiol. 106, 1241-1255.
    • (1994) Plant Physiol. , vol.106 , pp. 1241-1255
    • Newman, T.1    De Bruijn, F.J.2    Green, P.3
  • 21
    • 0005112214 scopus 로고
    • Expression of cloned genes in yeast
    • Glover, D.M. and Hames, B.D., eds. Oxford: Oxford University Press
    • Romanos, M.A., Scorer, C.A. and Clare, J.J. (1995) Expression of cloned genes in yeast. In: DNA Cloning 2 Expression Systems (Glover, D.M. and Hames, B.D., eds). Oxford: Oxford University Press. pp. 123-169.
    • (1995) DNA Cloning 2 Expression Systems , pp. 123-169
    • Romanos, M.A.1    Scorer, C.A.2    Clare, J.J.3
  • 23
    • 0342480428 scopus 로고
    • The role of maltase in the enzymolysis of raw starch
    • Schwimmer, S. (1945) The role of maltase in the enzymolysis of raw starch. J. Biol. Chem. 161, 219-234.
    • (1945) J. Biol. Chem. , vol.161 , pp. 219-234
    • Schwimmer, S.1
  • 24
    • 0000770846 scopus 로고
    • Rapid analysis of plant gene expression by a novel reverse transcriptase-PCR method
    • Simpson, C.G., Sinibaldi, R. and Brown, J.W.S. (1992) Rapid analysis of plant gene expression by a novel reverse transcriptase-PCR method. Plant J. 2, 835-836.
    • (1992) Plant J. , vol.2 , pp. 835-836
    • Simpson, C.G.1    Sinibaldi, R.2    Brown, J.W.S.3
  • 25
    • 0011879087 scopus 로고
    • Studies on wheat starch. II. the action of amylases on raw wheat starches
    • Stamberg, O.E. and Bailey, C.H. (1939) Studies on wheat starch. II. The action of amylases on raw wheat starches. Cereal Chem. 16, 319-330.
    • (1939) Cereal Chem. , vol.16 , pp. 319-330
    • Stamberg, O.E.1    Bailey, C.H.2
  • 27
    • 0031106232 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA encoding α-glucosidase from spinach
    • Sugimoto, M., Furui, S. and Suzuki, Y. (1997) Molecular cloning and characterization of a cDNA encoding α-glucosidase from spinach. Plant Mol. Biol. 33, 765-768.
    • (1997) Plant Mol. Biol. , vol.33 , pp. 765-768
    • Sugimoto, M.1    Furui, S.2    Suzuki, Y.3
  • 28
    • 0028843003 scopus 로고
    • The role of pea chloroplast α-glucosidase in transitory starch degradation
    • Sun, Z., Duke, S.H. and Henson, C.A. (1995) The role of pea chloroplast α-glucosidase in transitory starch degradation. Plant Physiol. 108, 211-217.
    • (1995) Plant Physiol. , vol.108 , pp. 211-217
    • Sun, Z.1    Duke, S.H.2    Henson, C.A.3
  • 29
    • 0000112493 scopus 로고
    • Degradation of native starch granules by barley α-glucosidases
    • Sun, Z. and Henson, C.A. (1990) Degradation of native starch granules by barley α-glucosidases. Plant Physiol. 94, 320-327.
    • (1990) Plant Physiol. , vol.94 , pp. 320-327
    • Sun, Z.1    Henson, C.A.2
  • 30
    • 0342923148 scopus 로고
    • Three forms of α-glucosidase from Welsh onion (Allium fistulosum L.)
    • Suzuki, Y. and Uchida, K. (1984) Three forms of α-glucosidase from Welsh onion (Allium fistulosum L.). Agric. Biol. Chem., 48, 1343-1345.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 1343-1345
    • Suzuki, Y.1    Uchida, K.2
  • 31
    • 0000433250 scopus 로고
    • Studies on α-glucosidase in rice. Part I. Isolation and some properties of α-glucosidase I and α-glucosidase II
    • Takahashi, M., Shimomura, T. and Chiba, S. (1971) Studies on α-glucosidase in rice. Part I. Isolation and some properties of α-glucosidase I and α-glucosidase II. Agric. Biol. Chem. 35, 2015-2024.
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 2015-2024
    • Takahashi, M.1    Shimomura, T.2    Chiba, S.3
  • 32
    • 0026949144 scopus 로고
    • Expression and sequence analysis of cDNAs induced during the early stages of tuberisation in different organs of the potato plant (Solanum tuberosum L.)
    • Taylor, M.A., Mad Arif, S.A., Kumar, A., Davies, H.V., Scobie, L.A., Pearce, S.R. and Flavell, A.J. (1992) Expression and sequence analysis of cDNAs induced during the early stages of tuberisation in different organs of the potato plant (Solanum tuberosum L.). Plant Mol. Biol. 20, 641-651.
    • (1992) Plant Mol. Biol. , vol.20 , pp. 641-651
    • Taylor, M.A.1    Mad Arif, S.A.2    Kumar, A.3    Davies, H.V.4    Scobie, L.A.5    Pearce, S.R.6    Flavell, A.J.7
  • 33
    • 0028535307 scopus 로고
    • Characterisation of the cDNA clones of two β-tubulin genes and their expression in the potato plant (Solanum tuberosum L.)
    • Taylor, M.A., Wright, F. and Davies, H.V. (1994) Characterisation of the cDNA clones of two β-tubulin genes and their expression in the potato plant (Solanum tuberosum L.). Plant Mol. Biol. 26, 1013-1018.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1013-1018
    • Taylor, M.A.1    Wright, F.2    Davies, H.V.3
  • 34
    • 0030050498 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a gibberellin-inducible putative α-glucosidase gene from barley
    • Tibbot, B.K. and Skadsen, R.W. (1996) Molecular cloning and characterization of a gibberellin-inducible putative α-glucosidase gene from barley. Plant Mol. Biol. 30, 229-241.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 229-241
    • Tibbot, B.K.1    Skadsen, R.W.2
  • 35
    • 0002669152 scopus 로고
    • A microplate reader assay for rapid enzymatic quantification of sugars in potato tubers
    • Viola, R. and Davies, H.V. (1992) A microplate reader assay for rapid enzymatic quantification of sugars in potato tubers. Potato Res. 35, 55-58.
    • (1992) Potato Res. , vol.35 , pp. 55-58
    • Viola, R.1    Davies, H.V.2
  • 36
    • 84934375932 scopus 로고
    • Two forms of α-glucosidase from soybean callus
    • Yamasaki, Y. and Konno, H. (1985) Two forms of α-glucosidase from soybean callus. Agric. Biol. Chem., 51, 3239-3244.
    • (1985) Agric. Biol. Chem. , vol.51 , pp. 3239-3244
    • Yamasaki, Y.1    Konno, H.2
  • 37
    • 6844238788 scopus 로고
    • Extracellular α-glucosidase from suspension-cultured sugar-beet cells
    • Yamasaki, Y. and Konno, H. (1991) Extracellular α-glucosidase from suspension-cultured sugar-beet cells. Agric. Biol. Chem., 55, 1675-1676.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1675-1676
    • Yamasaki, Y.1    Konno, H.2
  • 38
    • 0342489007 scopus 로고
    • Purification and properties of three α-glucosidases from germinated green gram (Phaseolus vidissimus Ten.)
    • Yamasaki, Y. and Suzuki, Y. (1979) Purification and properties of three α-glucosidases from germinated green gram (Phaseolus vidissimus Ten.) Agric. Biol. Chem., 43, 481-489.
    • (1979) Agric. Biol. Chem. , vol.43 , pp. 481-489
    • Yamasaki, Y.1    Suzuki, Y.2
  • 39
    • 0343358332 scopus 로고
    • Two forms of α-glucosidase from sugar beet seeds
    • Yamasaki, Y. and Suzuki, Y. (1980) Two forms of α-glucosidase from sugar beet seeds. Planta, 148, 354-361.
    • (1980) Planta , vol.148 , pp. 354-361
    • Yamasaki, Y.1    Suzuki, Y.2
  • 40
    • 85006097325 scopus 로고
    • Classification of some α-glucosidases and α-xylosidases on the basis of substrate specificity
    • Yoshikawa, K., Yamamoto, K. and Shigetaka, O. (1994) Classification of some α-glucosidases and α-xylosidases on the basis of substrate specificity. Biosci. Biotech., Biochem. 58, 1392-1398.
    • (1994) Biosci. Biotech., Biochem. , vol.58 , pp. 1392-1398
    • Yoshikawa, K.1    Yamamoto, K.2    Shigetaka, O.3


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