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Volumn 45, Issue 4, 2002, Pages 429-440

β-amylase in developing apple fruits: Activities, amounts and subcellular localization

Author keywords

amylase; Apple fruit; Subcellular localization; Western blotting

Indexed keywords

CELLS; DEGRADATION; ENZYME KINETICS; FRUITS; SEED; STARCH;

EID: 33645286118     PISSN: 10069305     EISSN: None     Source Type: Journal    
DOI: 10.1360/02yc9048     Document Type: Article
Times cited : (14)

References (66)
  • 1
    • 0000303823 scopus 로고
    • Sugar accumulation and changes in the activities of related enzymes during development of apple fruit
    • Beruter, J., Sugar accumulation and changes in the activities of related enzymes during development of apple fruit, J. Plant Physiol., 1985, 121: 331-334.
    • (1985) J. Plant Physiol. , vol.121 , pp. 331-334
    • Beruter, J.1
  • 4
    • 0000860075 scopus 로고
    • Molecular and cellular biology associated with endosperm mobilization in germinating cereal grains
    • Fincher, G. B., Molecular and cellular biology associated with endosperm mobilization in germinating cereal grains, Ann. Rev. Plant Physiol. Plant Mol. Biol., 1989, 40: 305-346.
    • (1989) Ann. Rev. Plant Physiol. Plant Mol. Biol. , vol.40 , pp. 305-346
    • Fincher, G.B.1
  • 5
    • 0001060540 scopus 로고
    • Quantitative and morphological studies on starch of apple fruit during development
    • Ohmiya, A., Kakiuchi, N., Quantitative and morphological studies on starch of apple fruit during development, J. Japan. Soc. Hort. Sci., 1990, 59: 417-423.
    • (1990) J. Japan. Soc. Hort. Sci. , vol.59 , pp. 417-423
    • Ohmiya, A.1    Kakiuchi, N.2
  • 6
    • 0001337123 scopus 로고
    • Distribution of amylases within sweet potato (Ipomoea batatas L.) root tissue
    • Hagenimana, V., Vezina, L. P., Simard, R. E., Distribution of amylases within sweet potato (Ipomoea batatas L.) root tissue, J. Agric. Food Chem., 1992, 40: 1777-1783.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 1777-1783
    • Hagenimana, V.1    Vezina, L.P.2    Simard, R.E.3
  • 7
    • 0000785628 scopus 로고
    • Sucrose synthase, starch accumulation, and tomato fruit sink strength
    • Wang, F., Sanz, A., Benner, M. L. et al., Sucrose synthase, starch accumulation, and tomato fruit sink strength, Plant Physiol., 1993, 101: 321-327.
    • (1993) Plant Physiol. , vol.101 , pp. 321-327
    • Wang, F.1    Sanz, A.2    Benner, M.L.3
  • 8
    • 0002733325 scopus 로고
    • Starch degradation and distribution of the starch-degrading enzymes in Vicia faba leaves
    • Ghiena, C., Schulz, M., Schnabl, H., Starch degradation and distribution of the starch-degrading enzymes in Vicia faba leaves, Plant Physiol., 1993, 101: 73-79.
    • (1993) Plant Physiol. , vol.101 , pp. 73-79
    • Ghiena, C.1    Schulz, M.2    Schnabl, H.3
  • 9
    • 0029108971 scopus 로고
    • Changes in amylase and total starch content in 'Fuji' apple during maturation
    • Fan, X., Matthesis, J. P., Patterson, M. E., Changes in amylase and total starch content in 'Fuji' apple during maturation, HortSci., 1995, 30: 104-105.
    • (1995) HortSci. , vol.30 , pp. 104-105
    • Fan, X.1    Matthesis, J.P.2    Patterson, M.E.3
  • 10
    • 0030755116 scopus 로고    scopus 로고
    • The effect of girdling on carbohydrate partitioning in the growing apple fruit
    • Beruter, J., Studer, M. E., Ruedi, P., The effect of girdling on carbohydrate partitioning in the growing apple fruit, J. Plant Physiol., 1997, 151: 77-285.
    • (1997) J. Plant Physiol. , vol.151 , pp. 77-285
    • Beruter, J.1    Studer, M.E.2    Ruedi, P.3
  • 11
    • 0031775207 scopus 로고    scopus 로고
    • Carbohydrate metabolism in ripening banana fruit
    • Prabha, T. N., Bhagyalakshmi, N., Carbohydrate metabolism in ripening banana fruit, Phytochemistry, 1998, 48: 915-919.
    • (1998) Phytochemistry , vol.48 , pp. 915-919
    • Prabha, T.N.1    Bhagyalakshmi, N.2
  • 13
    • 0035028356 scopus 로고    scopus 로고
    • Inhibition of β-amylase activity, starch degradation and sucrose formation by indole-3-acetic acid during banana ripening
    • Purgatto, E., Lajolo, F. M., do Nascimento, J. R. O. et al., Inhibition of β-amylase activity, starch degradation and sucrose formation by indole-3-acetic acid during banana ripening, Planta, 2001, 212: 823-828.
    • (2001) Planta , vol.212 , pp. 823-828
    • Purgatto, E.1    Lajolo, F.M.2    Do Nascimento, J.R.O.3
  • 14
    • 0001765463 scopus 로고
    • A model for starch breakdown in higher plants
    • Dunn, G. A., A model for starch breakdown in higher plants, Phytochemistry, 1974, 13: 1341-1346.
    • (1974) Phytochemistry , vol.13 , pp. 1341-1346
    • Dunn, G.A.1
  • 15
    • 0017896120 scopus 로고
    • Digestion of barley starch granules by the combined action of α- and β-amylases purified from barley and barley walt
    • Maeda, I., Kiribuchi, S., Nakamura, M., Digestion of barley starch granules by the combined action of α- and β-amylases purified from barley and barley walt, Agric. Biol. Chem., 1978, 42: 259-267.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 259-267
    • Maeda, I.1    Kiribuchi, S.2    Nakamura, M.3
  • 16
    • 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., 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. Biophys., 1991, 284: 298-305.
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 298-305
    • Sun, Z.1    Henson, C.A.2
  • 17
    • 0033958836 scopus 로고    scopus 로고
    • Comparison of degradation abilities of α- and β-amylases on raw starch granules
    • Sarikaya, E., Higasa, H., Adachi, M. et al., Comparison of degradation abilities of α- and β-amylases on raw starch granules, Process Biochem., 2000, 35: 711-715.
    • (2000) Process Biochem. , vol.35 , pp. 711-715
    • Sarikaya, E.1    Higasa, H.2    Adachi, M.3
  • 18
    • 0032143523 scopus 로고    scopus 로고
    • A starch accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch-hydrolyzing enzyme
    • Zeeman, S. C., Northrop, F., Smith, A. M. et al., A starch accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch-hydrolyzing enzyme, Plant J., 1998, 15: 357-365.
    • (1998) Plant J. , vol.15 , pp. 357-365
    • Zeeman, S.C.1    Northrop, F.2    Smith, A.M.3
  • 19
    • 0000603887 scopus 로고
    • Purification and characterization of pea epicotyl β-amylase
    • Lizzotte, P. A., Henson, C. A., Duke, S. H., Purification and characterization of pea epicotyl β-amylase. Plant Physiol., 1990, 92: 615-621.
    • (1990) Plant Physiol. , vol.92 , pp. 615-621
    • Lizzotte, P.A.1    Henson, C.A.2    Duke, S.H.3
  • 20
    • 0033389259 scopus 로고    scopus 로고
    • An Arabidopsis gene encoding a chloroplast-targeted-β amylase
    • Lao, N. T., Schoneveld, O., Mould, R. M. et al., An Arabidopsis gene encoding a chloroplast-targeted-β amylase, Plant J., 1999, 20: 519-528.
    • (1999) Plant J. , vol.20 , pp. 519-528
    • Lao, N.T.1    Schoneveld, O.2    Mould, R.M.3
  • 21
    • 0023657286 scopus 로고
    • Primary structure and differential expression of β-amylase in normal and mutants barley
    • Kreis, M., Williamson, M., Buxton, B. et al., Primary structure and differential expression of β-amylase in normal and mutants barley, Eur. J. Biochem., 1987, 169: 517-525.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 517-525
    • Kreis, M.1    Williamson, M.2    Buxton, B.3
  • 22
    • 12044250881 scopus 로고
    • Nucleotide sequence of a cDNA clone encoding a β-amylase from Arabidopsis thaliana
    • Monroe, J. D., Salminen, M. D., Preiss, J., Nucleotide sequence of a cDNA clone encoding a β-amylase from Arabidopsis thaliana, Plant Physiol., 1991, 97: 1599-1601.
    • (1991) Plant Physiol. , vol.97 , pp. 1599-1601
    • Monroe, J.D.1    Salminen, M.D.2    Preiss, J.3
  • 23
    • 0025824550 scopus 로고
    • Molecular cloning and expression in Escherichia coli of cDNA encoding the subunit of sweet potato β-amylase
    • Yoshida, N., Nakamura, K., Molecular cloning and expression in Escherichia coli of cDNA encoding the subunit of sweet potato β-amylase, J. Biochem., 1991, 110: 196-201.
    • (1991) J. Biochem. , vol.110 , pp. 196-201
    • Yoshida, N.1    Nakamura, K.2
  • 24
    • 0015527357 scopus 로고
    • The hydrolysis of maltodextrin by a β-amylase isolated from leaves of Vicia faba
    • Chapman, G. W., Pallas, J. E., Mendiceno, D., The hydrolysis of maltodextrin by a β-amylase isolated from leaves of Vicia faba, Biochim. Biophys. Acta, 1972, 276: 491-507.
    • (1972) Biochim. Biophys. Acta , vol.276 , pp. 491-507
    • Chapman, G.W.1    Pallas, J.E.2    Mendiceno, D.3
  • 25
    • 0001004433 scopus 로고
    • Subcellular localization of starch degradative and biosynthetic enzymes of spinach leaves
    • Okita, T. W., Greenberg, E., Kuhn, D. N. et al., Subcellular localization of starch degradative and biosynthetic enzymes of spinach leaves, Plant Physiol., 1979, 64: 187-192.
    • (1979) Plant Physiol. , vol.64 , pp. 187-192
    • Okita, T.W.1    Greenberg, E.2    Kuhn, D.N.3
  • 26
    • 0000627174 scopus 로고
    • Localization of starch biosynthesis and degradative enzymes in maize leaves
    • Echeverria, E., Boyer, C. D., Localization of starch biosynthesis and degradative enzymes in maize leaves, Am. J. Bot., 1986, 167-171.
    • (1986) Am. J. Bot. , pp. 167-171
    • Echeverria, E.1    Boyer, C.D.2
  • 27
    • 0001612521 scopus 로고
    • Water stress enhances expression of an α-amylase gene in barley leaves
    • Jacobsen, J. V., Hanson, A. D., Chandler, P. C., Water stress enhances expression of an α-amylase gene in barley leaves, Plant Physiol., 1986, 80: 350-359.
    • (1986) Plant Physiol. , vol.80 , pp. 350-359
    • Jacobsen, J.V.1    Hanson, A.D.2    Chandler, P.C.3
  • 28
    • 0001614498 scopus 로고
    • Exoamylase activity in vacuoles isolated from pea and wheat leaf protoplasts
    • Ziegler, P., Beck, E., Exoamylase activity in vacuoles isolated from pea and wheat leaf protoplasts, Plant Physiol., 1986, 82: 1119-1121.
    • (1986) Plant Physiol. , vol.82 , pp. 1119-1121
    • Ziegler, P.1    Beck, E.2
  • 29
    • 0000424878 scopus 로고
    • Chloroplast and extrachloroplastic starch-degrading enzymes in Pisum sativum L.
    • Kakefuda, G., Duke, S. H., Hostak, M. S., Chloroplast and extrachloroplastic starch-degrading enzymes in Pisum sativum L., Planta, 1986, 168: 175-182.
    • (1986) Planta , vol.168 , pp. 175-182
    • Kakefuda, G.1    Duke, S.H.2    Hostak, M.S.3
  • 30
    • 0000231796 scopus 로고
    • Subcellular localization and characterization of amylases in Arabidopsis leaf
    • Lin, T. P., Spilatro, S. R., Preiss, J., Subcellular localization and characterization of amylases in Arabidopsis leaf, Plant Physiol., 1988, 88: 251-259.
    • (1988) Plant Physiol. , vol.88 , pp. 251-259
    • Lin, T.P.1    Spilatro, S.R.2    Preiss, J.3
  • 31
    • 0001272522 scopus 로고
    • Partial purification and characterization of the major endoamylase of mature pea leaves
    • Ziegler, P., Partial purification and characterization of the major endoamylase of mature pea leaves, Plant Physiol., 1988, 86: 659-666.
    • (1988) Plant Physiol. , vol.86 , pp. 659-666
    • Ziegler, P.1
  • 32
    • 0000047235 scopus 로고
    • Altered regulation of β-amylase activity in mutants of Arabidopsis with lesions in starch metabolism
    • Caspar, T., Lin, T. P., Monroe, J. et al., Altered regulation of β-amylase activity in mutants of Arabidopsis with lesions in starch metabolism, Proc. Natl. Acad. Sci. USA, 1989, 86: 5830-5833.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5830-5833
    • Caspar, T.1    Lin, T.P.2    Monroe, J.3
  • 33
    • 0001372333 scopus 로고
    • Characterization of pea chloroplast D-enzyme (4-α-D- glucanotransferase)
    • Kakefuda, G., Duke, S. H., Characterization of pea chloroplast D-enzyme (4-α-D-glucanotransferase), Plant Physiol., 1989, 91: 136-143.
    • (1989) Plant Physiol. , vol.91 , pp. 136-143
    • Kakefuda, G.1    Duke, S.H.2
  • 34
    • 0009466084 scopus 로고
    • Purification of a β-amylase that accumulates in Arabidopsis thaliana mutants defective in starch metabolism
    • Monroe, J. D., Preiss, J., Purification of a β-amylase that accumulates in Arabidopsis thaliana mutants defective in starch metabolism, Plant Physiol., 1990, 94: 1033-1039.
    • (1990) Plant Physiol. , vol.94 , pp. 1033-1039
    • Monroe, J.D.1    Preiss, J.2
  • 35
    • 0031448938 scopus 로고    scopus 로고
    • Starch metabolism in developing embryos of oilseed rape
    • Da-Silva, P. M. F. R., Eastmond, P. J., Hill, L. M. et al., Starch metabolism in developing embryos of oilseed rape, Planta, 1997, 203: 480-487.
    • (1997) Planta , vol.203 , pp. 480-487
    • Da-Silva, P.M.F.R.1    Eastmond, P.J.2    Hill, L.M.3
  • 36
    • 0006181574 scopus 로고
    • Phytochrome-mediated regulation of β-amylase mRNA level in mustard (Sinapis alba L.) cotyledons
    • Sharma, R., Schopfer, P., Phytochrome-mediated regulation of β-amylase mRNA level in mustard (Sinapis alba L.) cotyledons, Planta, 1987, 171: 313-320.
    • (1987) Planta , vol.171 , pp. 313-320
    • Sharma, R.1    Schopfer, P.2
  • 37
    • 0042703039 scopus 로고
    • Lack of functional interrelationship between β-amylase photoregulation and chloroplast development in mustard (Sinapis alba L.) cotyledons
    • Manga, V. A., Sharma, R., Lack of functional interrelationship between β-amylase photoregulation and chloroplast development in mustard (Sinapis alba L.) cotyledons, Plant Cell Physiol., 1990, 31: 167-172.
    • (1990) Plant Cell Physiol. , vol.31 , pp. 167-172
    • Manga, V.A.1    Sharma, R.2
  • 38
    • 0041701300 scopus 로고
    • Amylases in pea tissues with reduced density and/or function
    • Saeed, M., Duck, S. H., Amylases in pea tissues with reduced density and/or function, Plant Physiol., 1990, 94: 1813-1819.
    • (1990) Plant Physiol. , vol.94 , pp. 1813-1819
    • Saeed, M.1    Duck, S.H.2
  • 39
    • 0001095351 scopus 로고
    • Sucrose-induced accumulation of β-amylase occurs concomitant with the accumulation of starch and sporamin in leaf-petiole cutting of sweet potato
    • Nakamura, K., Ohto, M., Yoshida, N. et al., Sucrose-induced accumulation of β-amylase occurs concomitant with the accumulation of starch and sporamin in leaf-petiole cutting of sweet potato, Plant Physiol., 1991, 96: 902-909.
    • (1991) Plant Physiol. , vol.96 , pp. 902-909
    • Nakamura, K.1    Ohto, M.2    Yoshida, N.3
  • 40
    • 0029257520 scopus 로고
    • Sugar-inducible expression of a gene for β-amylase in Arabidopsis thaliana
    • Mita, S., Suzuki-Fujii, K., Nakamura, K., Sugar-inducible expression of a gene for β-amylase in Arabidopsis thaliana, Plant Physiol., 1995, 107: 895-904.
    • (1995) Plant Physiol. , vol.107 , pp. 895-904
    • Mita, S.1    Suzuki-Fujii, K.2    Nakamura, K.3
  • 41
    • 0031153932 scopus 로고    scopus 로고
    • Negative regulation in the expression of a sugar-inducible gene in Arabidopsis thaliana
    • Mita, S., Hirano, H., Nakamura, K., Negative regulation in the expression of a sugar-inducible gene in Arabidopsis thaliana. Plant Physiol., 1997, 114: 575-582.
    • (1997) Plant Physiol. , vol.114 , pp. 575-582
    • Mita, S.1    Hirano, H.2    Nakamura, K.3
  • 42
    • 84985316652 scopus 로고
    • A simple colorimetric method for determination of sugar in fruit and vegetables
    • Blakeney, A. B., Mutton, L. L., A simple colorimetric method for determination of sugar in fruit and vegetables, J. Sci. Food Agri., 1980, 31: 889-897.
    • (1980) J. Sci. Food Agri. , vol.31 , pp. 889-897
    • Blakeney, A.B.1    Mutton, L.L.2
  • 43
    • 12044260049 scopus 로고
    • Sucrose phosphate synthase, sucrose synthase and invertase activities in developing fruit of Lycopersicon esculentum Mill, and the sucrose accumulating Lycopersicon hirsutum Humb. and bonp
    • Miron, D., Schaffer, A. A., Sucrose phosphate synthase, sucrose synthase and invertase activities in developing fruit of Lycopersicon esculentum Mill, and the sucrose accumulating Lycopersicon hirsutum Humb. and bonp., Plant Physiol., 1991, 95: 623-627.
    • (1991) Plant Physiol. , vol.95 , pp. 623-627
    • Miron, D.1    Schaffer, A.A.2
  • 44
    • 84985232904 scopus 로고
    • Sweet potato α- and β-amylase: Characterization and kinetic studies with endogenous inhibitors
    • Hagenimana, V., Vezine, L. P., Simard, R. E., Sweet potato α- and β-amylase: characterization and kinetic studies with endogenous inhibitors, J. Food Sci., 1994, 2: 373-377.
    • (1994) J. Food Sci. , vol.2 , pp. 373-377
    • Hagenimana, V.1    Vezine, L.P.2    Simard, R.E.3
  • 45
    • 0000510503 scopus 로고
    • Localization of branching enzyme in potato tuber cell with the use of immunoelectron microscopy
    • Kram, A. M., Oostergetel, G. T., Bruggen, E. F., Localization of branching enzyme in potato tuber cell with the use of immunoelectron microscopy, Plant Physiol., 1993, 101: 237-243.
    • (1993) Plant Physiol. , vol.101 , pp. 237-243
    • Kram, A.M.1    Oostergetel, G.T.2    Bruggen, E.F.3
  • 47
    • 0032146364 scopus 로고    scopus 로고
    • Hydrolysis of sucrose within isolated vacuoles from Solatium tuberosum L. tubers
    • Isla, M. I., Vattuone, M. A., Sampietro, A. R., Hydrolysis of sucrose within isolated vacuoles from Solatium tuberosum L. tubers, Planta, 1998, 205: 601-605.
    • (1998) Planta , vol.205 , pp. 601-605
    • Isla, M.I.1    Vattuone, M.A.2    Sampietro, A.R.3
  • 48
    • 0000999944 scopus 로고
    • β-amylase in germinating maize grains: Purification, characterization and antigenic relationships
    • Doyen, C., Lautiere, C., β-amylase in germinating maize grains: purification, characterization and antigenic relationships, Phytochemistry, 1992, 31: 3697-3702.
    • (1992) Phytochemistry , vol.31 , pp. 3697-3702
    • Doyen, C.1    Lautiere, C.2
  • 49
    • 0029411651 scopus 로고
    • Identification and characterization of a phloem-specific β-amylase
    • Wang, Q., Monroe, J., Sjolund, R. D., Identification and characterization of a phloem-specific β-amylase, Plant Physiol., 1995, 109: 743-750.
    • (1995) Plant Physiol. , vol.109 , pp. 743-750
    • Wang, Q.1    Monroe, J.2    Sjolund, R.D.3
  • 50
    • 84986859446 scopus 로고
    • Comparative immunological and chromatographic study of some plant β-amylase
    • Nummi, M., Daussant, J., Niku-Paavola, M. L. et al., Comparative immunological and chromatographic study of some plant β-amylase, J. Sci. Fd. Agric., 1970, 21: 258-261.
    • (1970) J. Sci. Fd. Agric. , vol.21 , pp. 258-261
    • Nummi, M.1    Daussant, J.2    Niku-Paavola, M.L.3
  • 51
    • 0042201776 scopus 로고
    • Starch phosphorylase inhibitor from sweet potato
    • Chang, T. C., Su, J. C., Starch phosphorylase inhibitor from sweet potato, Plant Physiol., 1986, 80: 534-538.
    • (1986) Plant Physiol. , vol.80 , pp. 534-538
    • Chang, T.C.1    Su, J.C.2
  • 52
    • 0007760415 scopus 로고
    • Starch phosphorylase inhibitor is β-amylase
    • Pan, S. M., Chang, T. C., Juang, R. H. et al., Starch phosphorylase inhibitor is β-amylase, Plant Physiol., 1988, 88: 1154-1156.
    • (1988) Plant Physiol. , vol.88 , pp. 1154-1156
    • Pan, S.M.1    Chang, T.C.2    Juang, R.H.3
  • 53
    • 84971795864 scopus 로고
    • Identification of a second locus encoding β-amylase on chromosome 2 of barley
    • Kreis, M., Williamson, M. S., Shewry, P. R. et al., Identification of a second locus encoding β-amylase on chromosome 2 of barley, Genet. Res., 1988, 51: 13-16.
    • (1988) Genet. Res. , vol.51 , pp. 13-16
    • Kreis, M.1    Williamson, M.S.2    Shewry, P.R.3
  • 54
    • 0001584686 scopus 로고
    • Induction of expression of genes coding sporamin and β-amylase by polygalacturonic acid in leaf-petiole cutting of sweet potato
    • Ohto, M., Nakamura-Kito, K., Nakamura, K., Induction of expression of genes coding sporamin and β-amylase by polygalacturonic acid in leaf-petiole cutting of sweet potato, Plant Physiol., 1992, 99: 422-427.
    • (1992) Plant Physiol. , vol.99 , pp. 422-427
    • Ohto, M.1    Nakamura-Kito, K.2    Nakamura, K.3
  • 55
    • 0029169548 scopus 로고
    • Spatial patterns of sucrose-induced and polygalacturonic acid-inducible expression of genes that encode sporamin and β-amylase in sweet potato
    • Tekada, S., Kowyama, Y., Takeuchi, Y. et al., Spatial patterns of sucrose-induced and polygalacturonic acid-inducible expression of genes that encode sporamin and β-amylase in sweet potato, Plant Cell Physiol., 1995, 36: 321-333.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 321-333
    • Tekada, S.1    Kowyama, Y.2    Takeuchi, Y.3
  • 56
    • 84913845038 scopus 로고
    • Immunohistochemical localization of β-amylase in resting barley seeds
    • Lauriere, C., Lauriere, M., Daussant, J., Immunohistochemical localization of β-amylase in resting barley seeds, Physiol. Plant., 1986, 67: 383-388.
    • (1986) Physiol. Plant. , vol.67 , pp. 383-388
    • Lauriere, C.1    Lauriere, M.2    Daussant, J.3
  • 57
    • 0000992348 scopus 로고
    • Conversion of free β-amylase to bound β-amylase on starch granules in the barley endosperm during desiccation phase of seed development
    • Hara-Nishimura, I., Nishimura, M., Daussant, J., Conversion of free β-amylase to bound β-amylase on starch granules in the barley endosperm during desiccation phase of seed development, Protoplasma, 1986, 134: 149-153.
    • (1986) Protoplasma , vol.134 , pp. 149-153
    • Hara-Nishimura, I.1    Nishimura, M.2    Daussant, J.3
  • 58
    • 85129724998 scopus 로고
    • Apple
    • (ed. Monselise, S. P.), Florida: CRC Press, Inc.
    • Dennis, F. G., Apple, in Handbook of Fruit Set and Development (ed. Monselise, S. P.), Florida: CRC Press, Inc., 1986, 1-44.
    • (1986) Handbook of Fruit Set and Development , pp. 1-44
    • Dennis, F.G.1
  • 59
    • 0009818401 scopus 로고    scopus 로고
    • Ultrastructure of epidermis and flesh of the developing apple fruit
    • Peng, Y. B., Zhang, D. P., Ultrastructure of epidermis and flesh of the developing apple fruit, Acta Bot. Sin., 2000, 42: 794 -802.
    • (2000) Acta Bot. Sin. , vol.42 , pp. 794-802
    • Peng, Y.B.1    Zhang, D.P.2
  • 60
    • 0001926095 scopus 로고    scopus 로고
    • Sugar unloading mechanism in the developing apple fruit
    • Lu, Y. M., Zhang, D. P., Yan, H. Y., Sugar unloading mechanism in the developing apple fruit, Acta Hortic. Sin. (in Chinese), 1999, 26: 141-146.
    • (1999) Acta Hortic. Sin. (In Chinese) , vol.26 , pp. 141-146
    • Lu, Y.M.1    Zhang, D.P.2    Yan, H.Y.3
  • 61
    • 0002899325 scopus 로고    scopus 로고
    • Ultrastructure of phloem and its surrounding parenchyma cells in the developing apple fruit
    • Lu, Y. M., Zhang, D. P., Yan, H. Y., Ultrastructure of phloem and its surrounding parenchyma cells in the developing apple fruit, Acta Bot. Sin. (in Chinese), 2000, 42: 32-42.
    • (2000) Acta Bot. Sin. (In Chinese) , vol.42 , pp. 32-42
    • Lu, Y.M.1    Zhang, D.P.2    Yan, H.Y.3
  • 62
    • 0034941231 scopus 로고    scopus 로고
    • Acid invertase is predominantly localized to cell walls of both the practically symplasmically isolated SE/CC complexes and parenchyma cells in developing apple fruit
    • Zhang, D. P., Lu, Y. M., Wang, Y. Z. et al., Acid invertase is predominantly localized to cell walls of both the practically symplasmically isolated SE/CC complexes and parenchyma cells in developing apple fruit, Plant, Cell & Environ., 2001, 24: 691-702.
    • (2001) Plant, Cell & Environ. , vol.24 , pp. 691-702
    • Zhang, D.P.1    Lu, Y.M.2    Wang, Y.Z.3
  • 63
    • 0000121123 scopus 로고
    • Osmoregulation and water stress in higher plant
    • Morgan, J. M., Osmoregulation and water stress in higher plant, Ann. Rev. Plant Physiol., 1984, 35: 299-319.
    • (1984) Ann. Rev. Plant Physiol. , vol.35 , pp. 299-319
    • Morgan, J.M.1
  • 64
    • 0001259470 scopus 로고
    • Metabolism and compartment of imported sugars in sink organs in relation to sink strength
    • Ho, L. C., Metabolism and compartment of imported sugars in sink organs in relation to sink strength, Ann. Rev. Plant Physiol. Plant Mol. Biol., 1988, 39: 355-378.
    • (1988) Ann. Rev. Plant Physiol. Plant Mol. Biol. , vol.39 , pp. 355-378
    • Ho, L.C.1
  • 65
    • 0001992141 scopus 로고
    • Changes in ethanol soluble carbohydrates during the development of two wheat cultivars subjected to different degrees of water stress
    • Drossopoulosl J. B., Karamanos, A. J., Niavis, C. A., Changes in ethanol soluble carbohydrates during the development of two wheat cultivars subjected to different degrees of water stress, J. Bot., 1987, 59: 173-180.
    • (1987) J. Bot. , vol.59 , pp. 173-180
    • Drossopoulosl, J.B.1    Karamanos, A.J.2    Niavis, C.A.3
  • 66
    • 85025535434 scopus 로고
    • Carbohydrate partitioning and changes in water relation of growing apple fruit
    • Beruter, J., Carbohydrate partitioning and changes in water relation of growing apple fruit, J. Plant Physiol., 1989, 135: 583-587.
    • (1989) J. Plant Physiol. , vol.135 , pp. 583-587
    • Beruter, J.1


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