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Volumn 89, Issue 1, 2007, Pages 49-62

Multiple forms of α-glucosidase in rice seeds (Oryza sativa L., var Nipponbare)

Author keywords

Glucosidase isoforms and isozymes; Glucosidase multigene family; Alternative splicing; Post translational proteolysis; Starch granules degradation

Indexed keywords

ALPHA GLUCOSIDASE; AMINO ACID; COMPLEMENTARY DNA; GENE PRODUCT; ISOENZYME; MESSENGER RNA; PEPTIDE; PROTEIN ONG1; PROTEIN ONG2; PROTEIN ONG2 I; PROTEIN ONG2 II; PROTEIN ONG3; PROTEIN ONG4; STARCH; VEGETABLE PROTEIN;

EID: 33845602014     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2006.09.014     Document Type: Article
Times cited : (25)

References (63)
  • 1
    • 0003532827 scopus 로고
    • The Handbook of Amylases and Related Enzymes
    • Pergamon Press, Oxford pp. 104-116
    • Chiba S. The Handbook of Amylases and Related Enzymes. The Amylase Research Society of Japan (1988), Pergamon Press, Oxford pp. 104-116
    • (1988) The Amylase Research Society of Japan
    • Chiba, S.1
  • 2
    • 0028886770 scopus 로고
    • Characterization of high pI α-glucosidase from germinated barley seeds: substrate specificity, subsite affinities and active-site residues
    • Im M., and Henson C.A. Characterization of high pI α-glucosidase from germinated barley seeds: substrate specificity, subsite affinities and active-site residues. Carbohydr. Res. 277 (1995) 145-159
    • (1995) Carbohydr. Res. , vol.277 , pp. 145-159
    • Im, M.1    Henson, C.A.2
  • 3
    • 0034126439 scopus 로고    scopus 로고
    • Purification, enzymatic characterization, and nucleotide sequence of high-isoelectric-point α-glucosidase from barley malt
    • Frandsen T.P., Lok F., Mirgorodskaya E., Roepstorff P., and Svensson B. Purification, enzymatic characterization, and nucleotide sequence of high-isoelectric-point α-glucosidase from barley malt. Plant Physiol. 123 (2000) 275-286
    • (2000) Plant Physiol. , vol.123 , pp. 275-286
    • Frandsen, T.P.1    Lok, F.2    Mirgorodskaya, E.3    Roepstorff, P.4    Svensson, B.5
  • 4
    • 0343221074 scopus 로고
    • Improved method for purification of buckwheat α-glucosidase and some kinetic properties
    • Kanaya K., Chiba S., Shimomura T., and Nishi K. Improved method for purification of buckwheat α-glucosidase and some kinetic properties. Agric. Biol. Chem. 40 (1976) 1929-1936
    • (1976) Agric. Biol. Chem. , vol.40 , pp. 1929-1936
    • Kanaya, K.1    Chiba, S.2    Shimomura, T.3    Nishi, K.4
  • 5
    • 84954960818 scopus 로고
    • Purification and some properties of flit corn α-glucosidase
    • Chiba S., and Shimomura T. Purification and some properties of flit corn α-glucosidase. Agric. Biol. Chem. 39 (1975) 1033-1040
    • (1975) Agric. Biol. Chem. , vol.39 , pp. 1033-1040
    • Chiba, S.1    Shimomura, T.2
  • 6
    • 85007803646 scopus 로고
    • Purification and substrate specificity of sweet corn α-glucosidase
    • Matsui H., Yazawa I., and Chiba S. Purification and substrate specificity of sweet corn α-glucosidase. Agric. Biol. Chem. 45 (1981) 887-894
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 887-894
    • Matsui, H.1    Yazawa, I.2    Chiba, S.3
  • 7
    • 0348236366 scopus 로고
    • Substrate specificity α-glucosidase II in rice seed
    • Murata S., Matsui H., and Chiba S. Substrate specificity α-glucosidase II in rice seed. Agric. Biol. Chem. 43 (1979) 2131-2135
    • (1979) Agric. Biol. Chem. , vol.43 , pp. 2131-2135
    • Murata, S.1    Matsui, H.2    Chiba, S.3
  • 8
    • 85009587911 scopus 로고
    • Substrate specificities of glutinous rice α-glucosidase I and α-glucosidase II
    • Ito H., Matsui H., and Chiba S. Substrate specificities of glutinous rice α-glucosidase I and α-glucosidase II. Denpun Kagaku 36 (1989) 189-195
    • (1989) Denpun Kagaku , vol.36 , pp. 189-195
    • Ito, H.1    Matsui, H.2    Chiba, S.3
  • 9
    • 0028890556 scopus 로고
    • Multiple molecular forms of α-glucosidase from spinacia seeds, Spinacia oleracea L
    • Sugimoto M., Furui S., and Suzuki Y. Multiple molecular forms of α-glucosidase from spinacia seeds, Spinacia oleracea L. Biosci. Biotechnol. Biochem. 59 (1995) 673-677
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 673-677
    • Sugimoto, M.1    Furui, S.2    Suzuki, Y.3
  • 10
    • 0007553835 scopus 로고
    • Purification and properties of an α-glucosidase in sugar beet seed
    • Matsui H., Chiba S., and Shimomura T. Purification and properties of an α-glucosidase in sugar beet seed. Agric. Biol. Chem. 42 (1978) 1855-1860
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 1855-1860
    • Matsui, H.1    Chiba, S.2    Shimomura, T.3
  • 11
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 (1991) 309-316
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 12
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B., and Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293 (1993) 781-788
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 13
    • 0026764917 scopus 로고
    • Action of neopullulanase: Neopullulanase catalyzes both hydrolysis and transglycosylation at α-(1→4)- and α-(1→6)-glucosidic linkages
    • Takata H., Kuriki T., Okada S., Takesada Y., Iizaka M., Minamiura N., and Imanaka T. Action of neopullulanase: Neopullulanase catalyzes both hydrolysis and transglycosylation at α-(1→4)- and α-(1→6)-glucosidic linkages. J. Biol. Chem. 267 (1992) 18447-18452
    • (1992) J. Biol. Chem. , vol.267 , pp. 18447-18452
    • Takata, H.1    Kuriki, T.2    Okada, S.3    Takesada, Y.4    Iizaka, M.5    Minamiura, N.6    Imanaka, T.7
  • 14
    • 0028429952 scopus 로고
    • Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability
    • Svensson B. Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol. 25 (1994) 141-157
    • (1994) Plant Mol. Biol. , vol.25 , pp. 141-157
    • Svensson, B.1
  • 15
    • 0035006850 scopus 로고    scopus 로고
    • Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe
    • Okuyama M., Okuno A., Shimizu N., Mori H., Kimura A., and Chiba S. Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe. Eur. J. Biochem. 268 (2001) 2270-2280
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2270-2280
    • Okuyama, M.1    Okuno, A.2    Shimizu, N.3    Mori, H.4    Kimura, A.5    Chiba, S.6
  • 16
    • 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. Molecular cloning and characterization of a gibberellin-inducible, putative α-glucosidase gene from barley. Plant Mol. Biol. 30 (1996) 229-241
    • (1996) Plant Mol. Biol. , vol.30 , pp. 229-241
    • Tibbot, B.K.1    Skadsen, R.W.2
  • 18
    • 0007112695 scopus 로고    scopus 로고
    • Nucleotide sequence of an α-glucosidase gene (Accession No. AF014806) from Arabidopsis thaliana
    • Monroe J.D., Hall B.D., Gough C.M., and Stephen A.L. Nucleotide sequence of an α-glucosidase gene (Accession No. AF014806) from Arabidopsis thaliana. Plant Physiol. 115 (1997) 863
    • (1997) Plant Physiol. , vol.115 , pp. 863
    • Monroe, J.D.1    Hall, B.D.2    Gough, C.M.3    Stephen, A.L.4
  • 19
    • 0031106232 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA encoding α-glucosidase from spinach
    • Sugimoto M., Furui S., and Suzuki Y. Molecular cloning and characterization of a cDNA encoding α-glucosidase from spinach. Plant Mol. Biol. 33 (1997) 765-768
    • (1997) Plant Mol. Biol. , vol.33 , pp. 765-768
    • Sugimoto, M.1    Furui, S.2    Suzuki, Y.3
  • 20
    • 0032005953 scopus 로고    scopus 로고
    • cDNA cloning and characterisation of an α-glucosidase gene from potato (Solanum tuberosum L.)
    • Taylor M.A., George L.A., Ross H.A., and Davies H.V. cDNA cloning and characterisation of an α-glucosidase gene from potato (Solanum tuberosum L.). Plant J. 13 (1998) 419-425
    • (1998) Plant J. , vol.13 , pp. 419-425
    • Taylor, M.A.1    George, L.A.2    Ross, H.A.3    Davies, H.V.4
  • 21
    • 0034931354 scopus 로고    scopus 로고
    • Copy-DNA cloning and characterization of a potato α-glucosidase: expression in Escherichia coli and effects of down-regulation in transgenic potato
    • Taylor M.A., Ross H.A., McRae D., Wright F., Viola R., and Davies H.V. Copy-DNA cloning and characterization of a potato α-glucosidase: expression in Escherichia coli and effects of down-regulation in transgenic potato. Planta 213 (2001) 258-264
    • (2001) Planta , vol.213 , pp. 258-264
    • Taylor, M.A.1    Ross, H.A.2    McRae, D.3    Wright, F.4    Viola, R.5    Davies, H.V.6
  • 22
    • 0001765463 scopus 로고
    • A model for starch breakdown in higher plants
    • Dunn G. A model for starch breakdown in higher plants. Phytochemistry 13 (1974) 1341-1346
    • (1974) Phytochemistry , vol.13 , pp. 1341-1346
    • Dunn, G.1
  • 23
    • 0031972297 scopus 로고    scopus 로고
    • Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin
    • Frandsen T.P., and Svensson B. Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin. Plant Mol. Biol. 37 (1998) 1-13
    • (1998) Plant Mol. Biol. , vol.37 , pp. 1-13
    • Frandsen, T.P.1    Svensson, B.2
  • 24
    • 0000112493 scopus 로고
    • Degradation of native starch granules by barley α-glucosidases
    • Sun Z., and Henson C.A. Degradation of native starch granules by barley α-glucosidases. Plant Physiol. 94 (1990) 320-327
    • (1990) Plant Physiol. , vol.94 , pp. 320-327
    • Sun, Z.1    Henson, C.A.2
  • 25
    • 0004670366 scopus 로고
    • Hydrolysis of barley starch granules by α-glucosidases from malts
    • Sissons M.J., and Macgregor A.W. Hydrolysis of barley starch granules by α-glucosidases from malts. J. Cereal Sci. 19 (1994) 161-169
    • (1994) J. Cereal Sci. , vol.19 , pp. 161-169
    • Sissons, M.J.1    Macgregor, A.W.2
  • 26
    • 0030038693 scopus 로고    scopus 로고
    • Purification and properties of α-glucosidase from millet seeds
    • Yamasaki Y., Konno H., and Masima H. Purification and properties of α-glucosidase from millet seeds. Phytochemistry 41 (1996) 703-705
    • (1996) Phytochemistry , vol.41 , pp. 703-705
    • Yamasaki, Y.1    Konno, H.2    Masima, H.3
  • 27
    • 0942291507 scopus 로고    scopus 로고
    • Relationship between the accumulation of starch and α-glucosidase in rice endosperm
    • Iwata H., Isogai A., Utsunomiya H., Itani T., and Nishio N. Relationship between the accumulation of starch and α-glucosidase in rice endosperm. Nippon Nougeikagaku kaishi 77 (2003) 1130-1136
    • (2003) Nippon Nougeikagaku kaishi , vol.77 , pp. 1130-1136
    • Iwata, H.1    Isogai, A.2    Utsunomiya, H.3    Itani, T.4    Nishio, N.5
  • 28
    • 17444370100 scopus 로고    scopus 로고
    • Purification and characterization of an α-glucosidase from germinating millet seeds
    • Yamasaki Y., Fujimoto M., Kariya J., and Konno H. Purification and characterization of an α-glucosidase from germinating millet seeds. Phytochemistry 66 (2005) 851-857
    • (2005) Phytochemistry , vol.66 , pp. 851-857
    • Yamasaki, Y.1    Fujimoto, M.2    Kariya, J.3    Konno, H.4
  • 29
    • 0026034124 scopus 로고
    • A quantitative assessment of the importance of barley seed α-amylase, β-amylase, debranching enzyme, and α-glucosidase in starch degradation
    • Sun Z.T., and Henson C.A. A quantitative assessment of the importance of barley seed α-amylase, β-amylase, debranching enzyme, and α-glucosidase in starch degradation. Arch. Biochem. 284 (1991) 298-305
    • (1991) Arch. Biochem. , vol.284 , pp. 298-305
    • Sun, Z.T.1    Henson, C.A.2
  • 30
    • 0343358332 scopus 로고
    • Two forms of α-glucosidase from sugar-beet seeds
    • Yoshiki Y., and Suzuki Y. Two forms of α-glucosidase from sugar-beet seeds. Planta 148 (1980) 354-361
    • (1980) Planta , vol.148 , pp. 354-361
    • Yoshiki, Y.1    Suzuki, Y.2
  • 31
    • 0032190488 scopus 로고    scopus 로고
    • Expression of enzymatically active, recombinant barley α-glucosidase in yeast and immunological detection of α-glucosidase from seed tissue
    • Tibbot B.K., Henson C.A., and Skadsen R.W. Expression of enzymatically active, recombinant barley α-glucosidase in yeast and immunological detection of α-glucosidase from seed tissue. Plant Mol. Biol. 38 (1998) 379-391
    • (1998) Plant Mol. Biol. , vol.38 , pp. 379-391
    • Tibbot, B.K.1    Henson, C.A.2    Skadsen, R.W.3
  • 33
    • 33845654628 scopus 로고
    • Purification and some properties of two α-glucosidases in glutinous rice seed
    • Ito H., Nakatsu S., Matsui H., and Chiba S. Purification and some properties of two α-glucosidases in glutinous rice seed. Denpun Kagaku 36 (1989) 181-187
    • (1989) Denpun Kagaku , vol.36 , pp. 181-187
    • Ito, H.1    Nakatsu, S.2    Matsui, H.3    Chiba, S.4
  • 34
    • 0000433250 scopus 로고
    • Studies on α-glucosidase in rice. Part I. Isolation and some properties of α-glucosidase I and α-glucosidase II
    • Takahashi N., Shimomura T., and Chiba S. Studies on α-glucosidase in rice. Part I. Isolation and some properties of α-glucosidase I and α-glucosidase II. Agric. Biol. Chem. 35 (1971) 2015-2024
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 2015-2024
    • Takahashi, N.1    Shimomura, T.2    Chiba, S.3
  • 35
    • 0942264355 scopus 로고    scopus 로고
    • Two forms of α-glucosidase from rice seeds at the milky stage
    • Yamasaki Y., and Suzuki Y. Two forms of α-glucosidase from rice seeds at the milky stage. Agric. Biol. Chem. 44 (1997) 707-715
    • (1997) Agric. Biol. Chem. , vol.44 , pp. 707-715
    • Yamasaki, Y.1    Suzuki, Y.2
  • 39
    • 0001707651 scopus 로고
    • Biochemical studies on buckwheat α-glucosidase part III. Transglucosylation action of the enzyme and isolation of the reaction products
    • Takahashi M., Shimomura T., and Chiba S. Biochemical studies on buckwheat α-glucosidase part III. Transglucosylation action of the enzyme and isolation of the reaction products. Agric. Biol. Chem. 33 (1969) 1399-1410
    • (1969) Agric. Biol. Chem. , vol.33 , pp. 1399-1410
    • Takahashi, M.1    Shimomura, T.2    Chiba, S.3
  • 40
    • 4644269533 scopus 로고
    • Quantitative determination of disaccharides produced from soluble starch through transglucosylation of buckwheat α-glucosidase
    • Chiba S., Kimura A., Kobori T., and Sitoh K. Quantitative determination of disaccharides produced from soluble starch through transglucosylation of buckwheat α-glucosidase. J. Jpn. Soc. Starch Sci. 32 (1985) 213-216
    • (1985) J. Jpn. Soc. Starch Sci. , vol.32 , pp. 213-216
    • Chiba, S.1    Kimura, A.2    Kobori, T.3    Sitoh, K.4
  • 41
    • 3543078738 scopus 로고    scopus 로고
    • Overexpression and characterization of two unknown proteins, YicI and YihQ, originated from Escherichia coli
    • Okuyama M., Mori H., Chiba S., and Kimura A. Overexpression and characterization of two unknown proteins, YicI and YihQ, originated from Escherichia coli. Protein Expr. 37 (2004) 170-179
    • (2004) Protein Expr. , vol.37 , pp. 170-179
    • Okuyama, M.1    Mori, H.2    Chiba, S.3    Kimura, A.4
  • 42
    • 0025358203 scopus 로고
    • Allosteric properties, substrate specificity, and subsite affinities of honeybee α-glucosidase I
    • Kimura A., Takewaki S., Matsui H., Kubota M., and Chiba S. Allosteric properties, substrate specificity, and subsite affinities of honeybee α-glucosidase I. J. Biochem. 107 (1990) 762-768
    • (1990) J. Biochem. , vol.107 , pp. 762-768
    • Kimura, A.1    Takewaki, S.2    Matsui, H.3    Kubota, M.4    Chiba, S.5
  • 43
    • 84958038063 scopus 로고
    • A photometric method for the determination of free pentoses in animal tissues
    • Roe J.H., and Rice E.W. A photometric method for the determination of free pentoses in animal tissues. J. Biol. Chem. 173 (1948) 507-512
    • (1948) J. Biol. Chem. , vol.173 , pp. 507-512
    • Roe, J.H.1    Rice, E.W.2
  • 44
    • 34250118553 scopus 로고
    • Xyloglucan (amyloid) mobilisation in the cotyledons of Tropaeolum majus L. seeds following germination
    • Edwards M., Dea I.C., Bulpin P.V., and Reid J.S. Xyloglucan (amyloid) mobilisation in the cotyledons of Tropaeolum majus L. seeds following germination. Planta 163 (1985) 133-140
    • (1985) Planta , vol.163 , pp. 133-140
    • Edwards, M.1    Dea, I.C.2    Bulpin, P.V.3    Reid, J.S.4
  • 45
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. 72 (1976) 248-254
    • (1976) Anal. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 46
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substrates
    • Dubois M., Gilles K.A., Hamilton J.K., Rebers P.A., and Smith F. Colorimetric method for determination of sugars and related substrates. Anal. Chem. 28 (1956) 350-356
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 47
    • 36949089946 scopus 로고
    • Disk electrophoresis of basic proteins and peptides on polyacrylamide gels
    • Reisfeld R.A., Lewis U.J., and Williams D.E. Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature 195 (1962) 281-283
    • (1962) Nature , vol.195 , pp. 281-283
    • Reisfeld, R.A.1    Lewis, U.J.2    Williams, D.E.3
  • 48
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-681
    • (1970) Nature , vol.227 , pp. 680-681
    • Laemmli, U.K.1
  • 49
    • 0000765113 scopus 로고
    • A rapid Smith-degradation for the determination of non-reducing, terminal residues of (1, 4)-α-d-glucans
    • Hizukuri S., and Osaki S. A rapid Smith-degradation for the determination of non-reducing, terminal residues of (1, 4)-α-d-glucans. Carbohydr. Res. 63 (1978) 261-264
    • (1978) Carbohydr. Res. , vol.63 , pp. 261-264
    • Hizukuri, S.1    Osaki, S.2
  • 50
    • 0000329882 scopus 로고
    • Multi-branched nature of amylose and the action of debranching enzymes
    • Hizukuri S., Takeda Y., Yasuda M., and Suzuki A. Multi-branched nature of amylose and the action of debranching enzymes. Carbohydr. Res. 94 (1981) 205-213
    • (1981) Carbohydr. Res. , vol.94 , pp. 205-213
    • Hizukuri, S.1    Takeda, Y.2    Yasuda, M.3    Suzuki, A.4
  • 51
    • 0016250949 scopus 로고
    • Magnesium precipitation of ribonucleoprotein complexes. Expedient techniques for the isolation of undergraded polysomes and messenger ribonucleic acid
    • Palmiter R.D. Magnesium precipitation of ribonucleoprotein complexes. Expedient techniques for the isolation of undergraded polysomes and messenger ribonucleic acid. Biochemistry 13 (1974) 3606-3615
    • (1974) Biochemistry , vol.13 , pp. 3606-3615
    • Palmiter, R.D.1
  • 52
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • Murray M.G., and Thompson W.F. Rapid isolation of high molecular weight plant DNA. Nucleic Acids Res. 8 (1980) 4321-4325
    • (1980) Nucleic Acids Res. , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 53
    • 0024026526 scopus 로고
    • Primary structure and processing of lysosomal α-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. Primary structure and processing of lysosomal α-glucosidase; homology with the intestinal sucrase-isomaltase complex. EMBO J. 7 (1988) 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
  • 54
    • 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. The sucrase-isomaltase complex: primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein. Cell 18 (1986) 227-234
    • (1986) Cell , vol.18 , pp. 227-234
    • Hunziker, W.1    Spiess, M.2    Semenza, G.3    Lodish, H.F.4
  • 57
    • 0034220797 scopus 로고    scopus 로고
    • The primary structure of the subunit in Bacillus thermoamyloliquefaciens KP071 molecular weight 540,000 homohexameric α-glucosidase II belonging to the glycosyl hydrolase family 31
    • Kashiwabara S., Azuma S., Tsuduki M., and Suzuki Y. The primary structure of the subunit in Bacillus thermoamyloliquefaciens KP071 molecular weight 540,000 homohexameric α-glucosidase II belonging to the glycosyl hydrolase family 31. Biosci. Biotechnol. Biochem. 64 (2000) 1379-1393
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1379-1393
    • Kashiwabara, S.1    Azuma, S.2    Tsuduki, M.3    Suzuki, Y.4
  • 58
    • 84969081579 scopus 로고
    • Low molecular-activity α-glucosidase from ungerminated rice seed
    • Matsui H., and Chiba S. Low molecular-activity α-glucosidase from ungerminated rice seed. Agric. Biol. Chem. 52 (1988) 1859-1860
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 1859-1860
    • Matsui, H.1    Chiba, S.2
  • 60
    • 33745048293 scopus 로고    scopus 로고
    • Structure of the Sulfolobus solfataricus α-glucosidase: implications for domain conservation and substrate recognition in GH31
    • Ernst H.A., Lo Leggio L., Willemoes M., Leonard G., Blum P., and Larsen S. Structure of the Sulfolobus solfataricus α-glucosidase: implications for domain conservation and substrate recognition in GH31. J. Mol. Biol. 358 (2006) 1106-1124
    • (2006) J. Mol. Biol. , vol.358 , pp. 1106-1124
    • Ernst, H.A.1    Lo Leggio, L.2    Willemoes, M.3    Leonard, G.4    Blum, P.5    Larsen, S.6
  • 61
    • 0026166257 scopus 로고
    • Differential expression of α-amylase genes in germinating rice and barley seeds
    • Karrer E.E., Litts J.C., and Rodriguez R.L. Differential expression of α-amylase genes in germinating rice and barley seeds. Plant Mol. Biol. 16 (1991) 797-805
    • (1991) Plant Mol. Biol. , vol.16 , pp. 797-805
    • Karrer, E.E.1    Litts, J.C.2    Rodriguez, R.L.3
  • 62
    • 0034989757 scopus 로고    scopus 로고
    • Cloning and expression pattern of a gene encoding an α-xylosidase active against xyloglucan oligosaccharides from Arabidopsis
    • Sampedro J., Sieiro C., Revilla G., Gonzalez-Villa T., and Zarra I. Cloning and expression pattern of a gene encoding an α-xylosidase active against xyloglucan oligosaccharides from Arabidopsis. Plant Physiol. 126 (2001) 910-920
    • (2001) Plant Physiol. , vol.126 , pp. 910-920
    • Sampedro, J.1    Sieiro, C.2    Revilla, G.3    Gonzalez-Villa, T.4    Zarra, I.5
  • 63
    • 0036938848 scopus 로고    scopus 로고
    • Molecular characterisation of a xyloglucan oligosaccharide-acting α-d-xylosidase from nasturtium (Tropaeolum majus L.) cotyledons that resembles plant 'apoplastic' α-d-glucosidases
    • Crombie H.J., Chengappa S., Jarman C., Sidebottom C., and Reid J.S. Molecular characterisation of a xyloglucan oligosaccharide-acting α-d-xylosidase from nasturtium (Tropaeolum majus L.) cotyledons that resembles plant 'apoplastic' α-d-glucosidases. Planta 214 (2002) 406-413
    • (2002) Planta , vol.214 , pp. 406-413
    • Crombie, H.J.1    Chengappa, S.2    Jarman, C.3    Sidebottom, C.4    Reid, J.S.5


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