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Volumn 8, Issue 7, 1996, Pages 1121-1135

Identification of the major starch synthase in the soluble fraction of potato tubers

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); SOLANUM TUBEROSUM;

EID: 0030198862     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.8.7.1121     Document Type: Article
Times cited : (114)

References (58)
  • 1
    • 0002583018 scopus 로고
    • Binary vectors
    • S.B. Gelvin and R.A. Schilperoort, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers)
    • An, G., Ebert, P.R., Mitra, A., and Ha, S.B. (1988). Binary vectors. In Plant Molecular Biology Manual A3, S.B. Gelvin and R.A. Schilperoort, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers), pp. 1-19.
    • (1988) Plant Molecular Biology Manual A3 , pp. 1-19
    • An, G.1    Ebert, P.R.2    Mitra, A.3    Ha, S.B.4
  • 2
    • 38249018749 scopus 로고
    • Properties of primer-dependent starch synthesis catalysed by starch synthase from potato tubers
    • Baba, T., Noro, M., Hiroto, M., and Arai, Y. (1990) Properties of primer-dependent starch synthesis catalysed by starch synthase from potato tubers. Phytochemistry 29, 719-723.
    • (1990) Phytochemistry , vol.29 , pp. 719-723
    • Baba, T.1    Noro, M.2    Hiroto, M.3    Arai, Y.4
  • 3
    • 0027675248 scopus 로고
    • Identification, cDNA cloning, and gene expression of soluble starch synthase in rice (Oryza sativa L.) immature seeds
    • Baba, T., Nishihara, M., Mizuno, K., Kawasaki, T., Shimada, H., Kobayashi, E., Ohnishi, S., Tanaka, K., and Arai, Y. (1993). Identification, cDNA cloning, and gene expression of soluble starch synthase in rice (Oryza sativa L.) immature seeds. Plant Physiol. 103, 565-573.
    • (1993) Plant Physiol. , vol.103 , pp. 565-573
    • Baba, T.1    Nishihara, M.2    Mizuno, K.3    Kawasaki, T.4    Shimada, H.5    Kobayashi, E.6    Ohnishi, S.7    Tanaka, K.8    Arai, Y.9
  • 4
    • 0021771482 scopus 로고
    • Binary Agrobacterium vectors for plant transformation
    • Bevan, M. (1984). Binary Agrobacterium vectors for plant transformation. Nucleic Acids Res. 12, 8711-8721.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 8711-8721
    • Bevan, M.1
  • 5
    • 0025101773 scopus 로고
    • The wrinkled-seed character of pea described by Mendel is caused by a transposon-like insertion in a gene encoding starch-branching enzyme
    • Bhattacharyya, M.K., Smith, A.M., Ellis, T.H.N., Medley, C., and Martin, C. (1990). The wrinkled-seed character of pea described by Mendel is caused by a transposon-like insertion in a gene encoding starch-branching enzyme. Cell 60, 115-122.
    • (1990) Cell , vol.60 , pp. 115-122
    • Bhattacharyya, M.K.1    Smith, A.M.2    Ellis, T.H.N.3    Medley, C.4    Martin, C.5
  • 7
    • 10144244142 scopus 로고
    • Comparison of soluble starch synthetase patterns in tubers and tuber-derived calli of Solanum tuberosum L
    • Catz, D.S., Moreno, S., and Tandecarz, J.S. (1989). Comparison of soluble starch synthetase patterns in tubers and tuber-derived calli of Solanum tuberosum L. An. Asoc. Quim. Argentina 77, 47-51
    • (1989) An. Asoc. Quim. Argentina , vol.77 , pp. 47-51
    • Catz, D.S.1    Moreno, S.2    Tandecarz, J.S.3
  • 8
    • 0026178941 scopus 로고
    • Nucleotide sequence of a wheat (Triticum aestivum) cDNA clone encoding the waxy protein
    • Clark, J.R., Robertson, M., and Ainsworth, C.C. (1991). Nucleotide sequence of a wheat (Triticum aestivum) cDNA clone encoding the waxy protein. Plant Mol. Biol. 16, 1099-1101.
    • (1991) Plant Mol. Biol. , vol.16 , pp. 1099-1101
    • Clark, J.R.1    Robertson, M.2    Ainsworth, C.C.3
  • 9
    • 0000198207 scopus 로고
    • Macromolecular structure of wrinkled- and smooth-pea starch components
    • Colonna, P., and Mercier, C. (1984). Macromolecular structure of wrinkled- and smooth-pea starch components. Carbohydr. Res. 126, 233-247.
    • (1984) Carbohydr. Res. , vol.126 , pp. 233-247
    • Colonna, P.1    Mercier, C.2
  • 10
    • 0001712485 scopus 로고
    • Gelatinization and melting of maize and pea starches with normal and high-amylose genotypes
    • Colonna, P., and Mercier C. (1985). Gelatinization and melting of maize and pea starches with normal and high-amylose genotypes. Phytochemistry 24, 1667-1674
    • (1985) Phytochemistry , vol.24 , pp. 1667-1674
    • Colonna, P.1    Mercier, C.2
  • 11
    • 0001016713 scopus 로고
    • The purification and characterisation of the two forms of soluble starch synthase from developing pea embryos
    • Denyer, K., and Smith, A.M. (1992). The purification and characterisation of the two forms of soluble starch synthase from developing pea embryos. Planta 186, 609-617.
    • (1992) Planta , vol.186 , pp. 609-617
    • Denyer, K.1    Smith, A.M.2
  • 12
    • 0027630893 scopus 로고
    • Soluble isoforms of starch synthase and starch-branching enzyme also occur within starch granules in developing pea embryos
    • Denyer, K., Sidebottom, C., Hylton, C.M., and Smith, A.M. (1993). Soluble isoforms of starch synthase and starch-branching enzyme also occur within starch granules in developing pea embryos. Plant J. 4, 191-198.
    • (1993) Plant J. , vol.4 , pp. 191-198
    • Denyer, K.1    Sidebottom, C.2    Hylton, C.M.3    Smith, A.M.4
  • 14
    • 0029168494 scopus 로고
    • Identification of multiple isoforms of soluble and granule-bound starch synthase in developing wheat endosperm
    • Denyer, K., Hylton, C.M., Jenner, C.F., and Smith, A.M. (1995b). Identification of multiple isoforms of soluble and granule-bound starch synthase in developing wheat endosperm. Planta 186, 256-265.
    • (1995) Planta , vol.186 , pp. 256-265
    • Denyer, K.1    Hylton, C.M.2    Jenner, C.F.3    Smith, A.M.4
  • 15
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P., and Smithies, O. (1984). A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12, 387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 16
    • 0026834195 scopus 로고
    • Characterization of cDNAs encoding two isoforms of granule-bound starch synthase which show differential expression in developing storage organs of pea and potato
    • Dry, I., Smith, A., Edwards, A., Bhattacharyya, M., Dunn, P., and Martin, C. (1992). Characterization of cDNAs encoding two isoforms of granule-bound starch synthase which show differential expression in developing storage organs of pea and potato. Plant J. 2, 193-202.
    • (1992) Plant J. , vol.2 , pp. 193-202
    • Dry, I.1    Smith, A.2    Edwards, A.3    Bhattacharyya, M.4    Dunn, P.5    Martin, C.6
  • 17
    • 0029347013 scopus 로고
    • Biochemical and molecular characterization of a novel starch synthase from potato tubers
    • Edwards, A., Marshall, J., Sidebottom, C., Visser, R.G.F., Smith, A.M., and Martin, C. (1995). Biochemical and molecular characterization of a novel starch synthase from potato tubers. Plant J. 8, 283-294.
    • (1995) Plant J. , vol.8 , pp. 283-294
    • Edwards, A.1    Marshall, J.2    Sidebottom, C.3    Visser, R.G.F.4    Smith, A.M.5    Martin, C.6
  • 18
    • 0014028939 scopus 로고
    • Studies on the biosynthesis of starch. I. Isolation and properties of the soluble adenosine diphosphate glucose:starch glucosyltransferase of Solanum tuberosum
    • Frydman, R.B., and Cardini, C.E. (1966). Studies on the biosynthesis of starch. I. Isolation and properties of the soluble adenosine diphosphate glucose:starch glucosyltransferase of Solanum tuberosum. Arch. Biochem. Biophys. 116, 9-18.
    • (1966) Arch. Biochem. Biophys. , vol.116 , pp. 9-18
    • Frydman, R.B.1    Cardini, C.E.2
  • 19
    • 0025078378 scopus 로고
    • Identification of lysine 15 at the active site in Escherichia coli glycogen synthase
    • Furukawa, K., Tagaya, M., Inoye, M., Preiss, J., and Fukui, T. (1990). Identification of lysine 15 at the active site in Escherichia coli glycogen synthase. J. Biol. Chem. 265, 2086-2090.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2086-2090
    • Furukawa, K.1    Tagaya, M.2    Inoye, M.3    Preiss, J.4    Fukui, T.5
  • 20
    • 0025135468 scopus 로고
    • A conserved cleavage-site motif in chloroplast transit peptides
    • Gavel, Y., and von Heinje, G. (1990). A conserved cleavage-site motif in chloroplast transit peptides. FEBS Lett. 261, 455-458.
    • (1990) FEBS Lett. , vol.261 , pp. 455-458
    • Gavel, Y.1    Von Heinje, G.2
  • 21
    • 51249167380 scopus 로고
    • Sucrose synthase catalyses a readily reversible reaction in vivo in developing potato tubers and other plant tissues
    • Geigenberger, P., and Stitt, M. (1993). Sucrose synthase catalyses a readily reversible reaction in vivo in developing potato tubers and other plant tissues. Planta 189, 329-339.
    • (1993) Planta , vol.189 , pp. 329-339
    • Geigenberger, P.1    Stitt, M.2
  • 22
    • 0027954143 scopus 로고
    • When growing potato tubers are detached from their mother plant there is a rapid inhibition of starch synthesis, involving inhibition of ADP-glucose pyrophosphorylase
    • Geigenberger, P., Merlo, L., Reimholz, R., and Stitt, M. (1934). When growing potato tubers are detached from their mother plant there is a rapid inhibition of starch synthesis, involving inhibition of ADP-glucose pyrophosphorylase. Planta 193, 486-493
    • (1934) Planta , vol.193 , pp. 486-493
    • Geigenberger, P.1    Merlo, L.2    Reimholz, R.3    Stitt, M.4
  • 23
    • 84987778390 scopus 로고
    • Plant transformation and expression vectors
    • R.R.D. Croy, ed (Oxford, UK: BIOS Scientific Publishers)
    • Guerineau, F., and Mullineaux, P. (1993). Plant transformation and expression vectors. In Plant Molecular Biology Labfax, R.R.D. Croy, ed (Oxford, UK: BIOS Scientific Publishers), pp. 121-148.
    • (1993) Plant Molecular Biology Labfax , pp. 121-148
    • Guerineau, F.1    Mullineaux, P.2
  • 24
    • 0028110601 scopus 로고
    • Transgenic potato plants with strongly decreased expression of pyrophosphate:fructose-6-phosphate phosphotransferase show no visible phenotype and only minor changes in tuber metabolism
    • Hajirezaei, M., Sonnewald, U., Viola, R., Carlisle, S., Dennis, D.T., and Stitt, M. (1993). Transgenic potato plants with strongly decreased expression of pyrophosphate:fructose-6-phosphate phosphotransferase show no visible phenotype and only minor changes in tuber metabolism Planta 192, 16-30.
    • (1993) Planta , vol.192 , pp. 16-30
    • Hajirezaei, M.1    Sonnewald, U.2    Viola, R.3    Carlisle, S.4    Dennis, D.T.5    Stitt, M.6
  • 25
    • 0001148138 scopus 로고
    • Unprimed starch synthesis by soluble ADPglucose-starch glucosyltransferase from potato tubers
    • Hawker, J.S., Ozbun, J.L., and Preiss, J. (1972) Unprimed starch synthesis by soluble ADPglucose-starch glucosyltransferase from potato tubers. Phytochemistry 11, 1278-1293.
    • (1972) Phytochemistry , vol.11 , pp. 1278-1293
    • Hawker, J.S.1    Ozbun, J.L.2    Preiss, J.3
  • 27
    • 0001506738 scopus 로고
    • 14C]sucrose in isolated wheat grains is dependent upon the activity of soluble starch synthase
    • 14C]sucrose in isolated wheat grains is dependent upon the activity of soluble starch synthase. Aust. J. Plant Physiol. 20, 329-335.
    • (1993) Aust. J. Plant Physiol. , vol.20 , pp. 329-335
    • Jenner, C.F.1    Siwek, K.2    Hawker, J.S.3
  • 28
    • 0027951459 scopus 로고
    • Caution on the use of the generally accepted methanol precipitation technique for the assay of soluble starch synthase in crude extracts of plant tissues
    • Jenner, C.F., Denyer, K., and Hawker, J.S. (1994). Caution on the use of the generally accepted methanol precipitation technique for the assay of soluble starch synthase in crude extracts of plant tissues. Aust. J. Plant Physiol. 21, 17-22
    • (1994) Aust. J. Plant Physiol. , vol.21 , pp. 17-22
    • Jenner, C.F.1    Denyer, K.2    Hawker, J.S.3
  • 29
    • 34250076038 scopus 로고
    • Elevated temperature reduces starch deposition in wheat endosperm by reducing the activity of soluble starch synthase
    • Keeling, P.L., Bacon, P.J., and Holt, D.C. (1993). Elevated temperature reduces starch deposition in wheat endosperm by reducing the activity of soluble starch synthase. Planta 191, 342-348.
    • (1993) Planta , vol.191 , pp. 342-348
    • Keeling, P.L.1    Bacon, P.J.2    Holt, D.C.3
  • 30
    • 0028174763 scopus 로고
    • Glycogen in Bacillus subtilis: Molecular characterization of an operon encoding enzymes involved in glycogen biosynthesis and degradation
    • Kiel, J.A., Boels, J.M., Beldman, G., and Venema, G. (1994). Glycogen in Bacillus subtilis: Molecular characterization of an operon encoding enzymes involved in glycogen biosynthesis and degradation. Mol. Microbiol. 11, 203-218.
    • (1994) Mol. Microbiol. , vol.11 , pp. 203-218
    • Kiel, J.A.1    Boels, J.M.2    Beldman, G.3    Venema, G.4
  • 32
    • 0027953123 scopus 로고
    • Formation and deposition of amylose in the potato tuber starch granule are affected by the reduction of granule-bound starch synthase gene expression
    • Kuipers, A.G.J., Jacobsen, E., and Visser, R.G.F. (1994). Formation and deposition of amylose in the potato tuber starch granule are affected by the reduction of granule-bound starch synthase gene expression. Plant Cell 6, 43-52.
    • (1994) Plant Cell , vol.6 , pp. 43-52
    • Kuipers, A.G.J.1    Jacobsen, E.2    Visser, R.G.F.3
  • 33
    • 0022993290 scopus 로고
    • Biosynthesis of bacterial glycogen: Primary structure of Escherichia coli ADP-glucose: α-1,4-glucan 4-glucosyltransferase as deduced from the nucleotide sequence of the g/gA gene
    • Kumar, A., Larsen, C.E., and Preiss, J. (1986). Biosynthesis of bacterial glycogen: Primary structure of Escherichia coli ADP-glucose: α-1,4-glucan 4-glucosyltransferase as deduced from the nucleotide sequence of the g/gA gene. J. Biol. Chem. 261, 16256-16259.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16256-16259
    • Kumar, A.1    Larsen, C.E.2    Preiss, J.3
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0029328417 scopus 로고
    • Starch biosynthesis
    • Martin, C., and Smith, A.M. (1995). Starch biosynthesis. Plant Cell 7, 971-985
    • (1995) Plant Cell , vol.7 , pp. 971-985
    • Martin, C.1    Smith, A.M.2
  • 36
    • 46149136757 scopus 로고
    • Sugar metabolism in developing tubers of Solanum tuberosum
    • Morrell, S., and ap Rees, T. (1986). Sugar metabolism in developing tubers of Solanum tuberosum. Phytochemistry 25, 1579-1585.
    • (1986) Phytochemistry , vol.25 , pp. 1579-1585
    • Morrell, S.1    Ap Rees, T.2
  • 37
    • 85016668976 scopus 로고
    • An improved colorimetric procedure for determining apparent and total amylose in cereal and other starches
    • Morrison, W.R., and Laignelet, B. (1983). An improved colorimetric procedure for determining apparent and total amylose in cereal and other starches. J. Cereal Sci. 1, 9-20.
    • (1983) J. Cereal Sci. , vol.1 , pp. 9-20
    • Morrison, W.R.1    Laignelet, B.2
  • 38
    • 0028083844 scopus 로고
    • Association of a 76 kDa polypeptide with soluble starch synthase I activity in maize (cv B73) endosperm
    • Mu, C., Harn, C., Ko, Y.T., Singletary, G.W., Keeling, P.L., and Wasserman, B.P. (1994). Association of a 76 kDa polypeptide with soluble starch synthase I activity in maize (cv B73) endosperm. Plant J. 6, 151-159.
    • (1994) Plant J. , vol.6 , pp. 151-159
    • Mu, C.1    Harn, C.2    Ko, Y.T.3    Singletary, G.W.4    Keeling, P.L.5    Wasserman, B.P.6
  • 39
    • 84994964585 scopus 로고
    • Approaches to influence starch quantity and starch quality in transgenic plants
    • Müller-Röber, B., and Kossmann, J. (1994). Approaches to influence starch quantity and starch quality in transgenic plants. Plant Cell Environ. 17, 601-613.
    • (1994) Plant Cell Environ. , vol.17 , pp. 601-613
    • Müller-Röber, B.1    Kossmann, J.2
  • 40
    • 0026877443 scopus 로고
    • Nucleotide sequence of a long cDNA from the rice waxy gene
    • Okagaki, R.J. (1992). Nucleotide sequence of a long cDNA from the rice waxy gene. Plant Mol. Biol. 19, 513-516.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 513-516
    • Okagaki, R.J.1
  • 41
    • 10144238044 scopus 로고
    • PhD Dissertation (Groningen, The Netherlands: State University of Groningen)
    • Ponstein, A. (1990) Starch Synthesis in Potato Tubers. PhD Dissertation (Groningen, The Netherlands: State University of Groningen).
    • (1990) Starch Synthesis in Potato Tubers
    • Ponstein, A.1
  • 42
    • 0024297043 scopus 로고
    • Structural analysis of the waxy locus from Hordeum vulgare
    • Rohde, W., Becker, D., and Salamini, F. (1988). Structural analysis of the waxy locus from Hordeum vulgare. Nucleic Acids Res. 16, 7185-7186.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7185-7186
    • Rohde, W.1    Becker, D.2    Salamini, F.3
  • 43
    • 0027762218 scopus 로고
    • Isolation and characterization of a cDNA encoding granule-bound starch synthase in cassava (Manihot esculenta Crantz) and its antisense expression in potato
    • Salehuzzaman, S.N.I.M., Jacobsen, E., and Visser, R.G.F. (1993). Isolation and characterization of a cDNA encoding granule-bound starch synthase in cassava (Manihot esculenta Crantz) and its antisense expression in potato. Plant Mol. Biol. 23, 947-962.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 947-962
    • Salehuzzaman, S.N.I.M.1    Jacobsen, E.2    Visser, R.G.F.3
  • 45
    • 0000507749 scopus 로고
    • Matrices for detecting distant relationships
    • M.O. Dayhoff, ed (Washington, DC: National Biomedical Research Foundation)
    • Schwartz, R.M., and Dayhoff, M.O. (1979). Matrices for detecting distant relationships. In Atlas of Protein Sequence and Structure, M.O. Dayhoff, ed (Washington, DC: National Biomedical Research Foundation), pp. 353-358.
    • (1979) Atlas of Protein Sequence and Structure , pp. 353-358
    • Schwartz, R.M.1    Dayhoff, M.O.2
  • 46
    • 0000797202 scopus 로고
    • Modifying starch biosynthesis with transgenes in potatoes
    • Shewmaker, C.K., and Stalker, D.M. (1992). Modifying starch biosynthesis with transgenes in potatoes. Plant Physiol. 100, 1083-1086.
    • (1992) Plant Physiol. , vol.100 , pp. 1083-1086
    • Shewmaker, C.K.1    Stalker, D.M.2
  • 47
    • 0001481929 scopus 로고
    • Major differences in isoforms of starch-branching enzyme in embryos of round- and wrinkled-seeded peas (Pisum sativum L.)
    • Smith, A.M. (1988) Major differences in isoforms of starch-branching enzyme in embryos of round- and wrinkled-seeded peas (Pisum sativum L.). Planta 175, 270-279.
    • (1988) Planta , vol.175 , pp. 270-279
    • Smith, A.M.1
  • 48
    • 0001253709 scopus 로고
    • Evidence that the "waxy" protein of pea (Pisum sativum L.) is not the major granule-bound starch synthase
    • Smith, A.M. (1990). Evidence that the "waxy" protein of pea (Pisum sativum L.) is not the major granule-bound starch synthase. Planta 182, 599-604.
    • (1990) Planta , vol.182 , pp. 599-604
    • Smith, A.M.1
  • 49
    • 0029138717 scopus 로고
    • What controls the amount and structure of starch in storage organs?
    • Smith, A.M., Denyer, K., and Martin, C.R. (1995) What controls the amount and structure of starch in storage organs? Plant Physiol. 107, 673-677.
    • (1995) Plant Physiol. , vol.107 , pp. 673-677
    • Smith, A.M.1    Denyer, K.2    Martin, C.R.3
  • 50
    • 84994995728 scopus 로고
    • Manipulation of sink-source relations in transgenic plants
    • Sonnewald, U., Lerchl, J., Zrenner, R., and Frommer, W. (1994). Manipulation of sink-source relations in transgenic plants Plant Cell Environ. 17, 649-658.
    • (1994) Plant Cell Environ. , vol.17 , pp. 649-658
    • Sonnewald, U.1    Lerchl, J.2    Zrenner, R.3    Frommer, W.4
  • 51
    • 0015988432 scopus 로고
    • The function of the waxy locus in starch synthesis in maize endosperm
    • Tsai, C.-Y. (1974). The function of the waxy locus in starch synthesis in maize endosperm. Biochem. Genet. 11, 83-96.
    • (1974) Biochem. Genet. , vol.11 , pp. 83-96
    • Tsai, C.-Y.1
  • 52
    • 0025228701 scopus 로고
    • Biochemical characterization of avirulent exoC mutants of Agrobacterium tumefaciens
    • Uttaro, A.D., Cangelosi, G.A., Geremia, R.A., Nester, E.W., and Ugalde, R.A. (1990). Biochemical characterization of avirulent exoC mutants of Agrobacterium tumefaciens. J. Bacteriol. 172, 1640-1646.
    • (1990) J. Bacteriol. , vol.172 , pp. 1640-1646
    • Uttaro, A.D.1    Cangelosi, G.A.2    Geremia, R.A.3    Nester, E.W.4    Ugalde, R.A.5
  • 53
    • 0025783787 scopus 로고
    • Sequence of the structural gene for granule-bound starch synthase of potato (Solanum tuberosum L.) and evidence for a single point deletion in the amf allele
    • van der Leij, F.R., Visser, R.G.F., Ponstein, A.S., Jacobsen, E., and Feenstra, W.J. (1991). Sequence of the structural gene for granule-bound starch synthase of potato (Solanum tuberosum L.) and evidence for a single point deletion in the amf allele. Mol. Gen. Genet. 228, 240-248.
    • (1991) Mol. Gen. Genet. , vol.228 , pp. 240-248
    • Van Der Leij, F.R.1    Visser, R.G.F.2    Ponstein, A.S.3    Jacobsen, E.4    Feenstra, W.J.5
  • 54
    • 0027551706 scopus 로고
    • Towards modifying plants for altered starch content and composition
    • Visser, R.G.F., and Jacobsen, E. (1993). Towards modifying plants for altered starch content and composition Trends Biotech. 11, 63-68.
    • (1993) Trends Biotech. , vol.11 , pp. 63-68
    • Visser, R.G.F.1    Jacobsen, E.2
  • 55
    • 0001898339 scopus 로고
    • Molecular cloning and partial characterisation of the gene for granule-bound starch synthase from a wild-type and an amylose-free potato (Solanum tuberosum L.)
    • Visser, R.G.F., Hergersberg, M., van der Leij, F.R., Jacobsen, E., Witholt, B., and Feenstra, W.J. (1989). Molecular cloning and partial characterisation of the gene for granule-bound starch synthase from a wild-type and an amylose-free potato (Solanum tuberosum L.). Plant Sci 64, 185-192
    • (1989) Plant Sci , vol.64 , pp. 185-192
    • Visser, R.G.F.1    Hergersberg, M.2    Van Der Leij, F.R.3    Jacobsen, E.4    Witholt, B.5    Feenstra, W.J.6
  • 56
    • 0026027970 scopus 로고
    • Inhibition of the expression of the gene for granule-bound starch synthase in potato by antisense constructs
    • Visser, R.G.F., Somhorst, I., Kuipers, G.J., Ruys, N.J., Feenstra, W.J., and Jacobsen, E. (1991) Inhibition of the expression of the gene for granule-bound starch synthase in potato by antisense constructs. Mol. Gen. Genet 225, 289-296
    • (1991) Mol. Gen. Genet , vol.225 , pp. 289-296
    • Visser, R.G.F.1    Somhorst, I.2    Kuipers, G.J.3    Ruys, N.J.4    Feenstra, W.J.5    Jacobsen, E.6
  • 58
    • 0016174534 scopus 로고
    • Immobilization of ligands for biospecific affinity chromatography via their hydroxyl groups. The cyclohexaamylose-β-amylase system
    • Vretblad, P. (1974). Immobilization of ligands for biospecific affinity chromatography via their hydroxyl groups. The cyclohexaamylose-β-amylase system. FEBS Lett. 47, 86-89.
    • (1974) FEBS Lett. , vol.47 , pp. 86-89
    • Vretblad, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.