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Volumn 31, Issue 3, 1996, Pages 657-672

Molecular cloning of the lectin and a lectin-related protein from common Solomon's seal (Polygonatum multiflorum)

Author keywords

cDNA cloning; lectin; lectin related protein; Polygonatum multiflorum; Solomon's seal

Indexed keywords

GALANTHUS; LILIACEAE; PHOCIDAE; POLYGONATUM MULTIFLORUM;

EID: 0030175540     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00042237     Document Type: Article
Times cited : (30)

References (43)
  • 2
    • 0025979184 scopus 로고
    • 9-(2-phosphonylmethoxyethyl)adenine (PMEA) effectively inhibits retrovirus replication in vitro and simian immunodeficiency virus infection in Rhesus monkeys
    • Balzarini J, Naesens L, Slachmuylders J, Niphuis H, Rosenberg I, Holy A, Schellekens H, De Clercq E: 9-(2-phosphonylmethoxyethyl)adenine (PMEA) effectively inhibits retrovirus replication in vitro and simian immunodeficiency virus infection in Rhesus monkeys. AIDS 5: 21-28 (1991).
    • (1991) AIDS , vol.5 , pp. 21-28
    • Balzarini, J.1    Naesens, L.2    Slachmuylders, J.3    Niphuis, H.4    Rosenberg, I.5    Holy, A.6    Schellekens, H.7    De Clercq, E.8
  • 3
    • 0026020005 scopus 로고
    • α-(1-3)- and α-(1-6)-D-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro
    • Balzarini J, Schols D, Neyts J, Van Damme E, Peumans W, De Clercq E: α-(1-3)- and α-(1-6)-D-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro. Antimicrob Agents Chemother 35: 410-416 (1991).
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 410-416
    • Balzarini, J.1    Schols, D.2    Neyts, J.3    Van Damme, E.4    Peumans, W.5    De Clercq, E.6
  • 4
    • 0026532965 scopus 로고
    • n -specific plant lectin from Urtica dioica are potent and selective inhibitors of human immunodeficiency virus and cytomegalovirus replication in vitro
    • n -specific plant lectin from Urtica dioica are potent and selective inhibitors of human immunodeficiency virus and cytomegalovirus replication in vitro. Antiviral Res 18: 191-207 (1992).
    • (1992) Antiviral Res , vol.18 , pp. 191-207
    • Balzarini, J.1    Neyts, J.2    Schols, D.3    Hosoya, M.4    Van Damme, E.5    Peumans, W.6    De Clercq, E.7
  • 6
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugar and related substances
    • Dubois M, Gilles KA, Hamilton JK, Rebers PA, Smith F: Colorimetric method for determination of sugar and related substances. Anal Chem 28: 350-356 (1956).
    • (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
  • 7
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gaboriaud C, Bissery V, Benchetrit T, Mornon JP: Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett 224: 149-155 (1987).
    • (1987) FEBS Lett , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 8
    • 0002199711 scopus 로고
    • Isolation, physicochemical characterization and carbohydrate binding specificity of lectins
    • Liener IE, Sharon N, Goldstein IJ (eds), Academic Press, New York
    • Goldstein IJ, Poretz RD: Isolation, physicochemical characterization and carbohydrate binding specificity of lectins. In Liener IE, Sharon N, Goldstein IJ (eds), The Lectins: Properties, Functions and Applications in Biology and Medicine, pp. 33-248, Academic Press, New York (1986).
    • (1986) The Lectins: Properties, Functions and Applications in Biology and Medicine , pp. 33-248
    • Goldstein, I.J.1    Poretz, R.D.2
  • 9
    • 0029008975 scopus 로고
    • Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family
    • Hester G, Kaku H, Goldstein IJ, Wright CS: Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family. Nature Struct Biol 2: 472-479 (1995).
    • (1995) Nature Struct Biol , vol.2 , pp. 472-479
    • Hester, G.1    Kaku, H.2    Goldstein, I.J.3    Wright, C.S.4
  • 11
    • 0000448982 scopus 로고
    • Prediction of protein antigenic determinants from amino acid sequences
    • Hopp TP, Woods KR: Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 78: 3824-3828 (1981).
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3824-3828
    • Hopp, T.P.1    Woods, K.R.2
  • 12
    • 0018784438 scopus 로고
    • Surface and inside volumes in globularproteins
    • Janin J: Surface and inside volumes in globularproteins. Nature 277: 491-192 (1979).
    • (1979) Nature , vol.277 , pp. 491-1192
    • Janin, J.1
  • 13
    • 0021918946 scopus 로고
    • Prediction of chain flexibility in proteins
    • Karplus PA, Schulz GE: Prediction of chain flexibility in proteins. Naturwissenschaften 72: 212-213 (1985).
    • (1985) Naturwissenschaften , vol.72 , pp. 212-213
    • Karplus, P.A.1    Schulz, G.E.2
  • 14
    • 0028978737 scopus 로고
    • The complete amino acid sequence of a mannose-binding lectin from 'Kidachi Aloe' (Aloe arborescens van Natalensis Berger)
    • Koike T, Titani K, Suzuki M, Beppu H, Kuzuya H, Maruta K, Shimpo K, Fujita K: The complete amino acid sequence of a mannose-binding lectin from 'Kidachi Aloe' (Aloe arborescens van Natalensis Berger). Biochem Biophys Res Commun 214: 163-170 (1995).
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 163-170
    • Koike, T.1    Titani, K.2    Suzuki, M.3    Beppu, H.4    Kuzuya, H.5    Maruta, K.6    Shimpo, K.7    Fujita, K.8
  • 15
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF: A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132 (1982).
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 17
    • 0025129872 scopus 로고
    • Hydrophobic cluster analysis: Procedure to derive structural and functional information from 2-D-representation of protein sequences
    • Lemesle-Varloot L, Henrissat B, Gaboriaud C, Bissery V, Morgat A, Mornon JP: Hydrophobic cluster analysis: procedure to derive structural and functional information from 2-D-representation of protein sequences. Biochimie 72: 555-574 (1990).
    • (1990) Biochimie , vol.72 , pp. 555-574
    • Lemesle-Varloot, L.1    Henrissat, B.2    Gaboriaud, C.3    Bissery, V.4    Morgat, A.5    Mornon, J.P.6
  • 19
    • 0023070284 scopus 로고
    • Direct sequencing of denatured plasmid DNA
    • Mierendorf RC, Pfeffer D: Direct sequencing of denatured plasmid DNA. Meth Enzymol 152: 556-562 (1987).
    • (1987) Meth Enzymol , vol.152 , pp. 556-562
    • Mierendorf, R.C.1    Pfeffer, D.2
  • 20
    • 0028534816 scopus 로고
    • Evolutionary relationships among proteins in the phytohemagglutinin-arcelin-α-amylase inhibitor family of the common bean and its relatives
    • Mirkov E, Wahlstrom JM, Hagiwara K, Finardi-Filho F, Kjemtrup S, Chrispeels MJ: Evolutionary relationships among proteins in the phytohemagglutinin-arcelin-α-amylase inhibitor family of the common bean and its relatives. Plant Mol Biol 26: 1103-1113 (1994).
    • (1994) Plant Mol Biol , vol.26 , pp. 1103-1113
    • Mirkov, E.1    Wahlstrom, J.M.2    Hagiwara, K.3    Finardi-Filho, F.4    Kjemtrup, S.5    Chrispeels, M.J.6
  • 21
    • 0022772926 scopus 로고
    • Isolation and characterization of a lectin from tulip bulbs, Tulipa gesneriana
    • Oda Y, Minami K: Isolation and characterization of a lectin from tulip bulbs, Tulipa gesneriana. Eur J Biochem 159: 239-245 (1986).
    • (1986) Eur J Biochem , vol.159 , pp. 239-245
    • Oda, Y.1    Minami, K.2
  • 22
    • 0023055775 scopus 로고
    • New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: Correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites
    • Parker JMR, Guo D, Hodges RS: New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites. Biochemistry 25: 5425-5432 (1986).
    • (1986) Biochemistry , vol.25 , pp. 5425-5432
    • Parker, J.M.R.1    Guo, D.2    Hodges, R.S.3
  • 23
    • 0011847928 scopus 로고
    • A new lectin from meadow saffron (Colchicum autumnale)
    • Peumans WJ, Allen AK, Cammue BP: A new lectin from meadow saffron (Colchicum autumnale). Plant Physiol 82: 1036-1039 (1986).
    • (1986) Plant Physiol , vol.82 , pp. 1036-1039
    • Peumans, W.J.1    Allen, A.K.2    Cammue, B.P.3
  • 26
    • 0027384516 scopus 로고
    • The alpha-mannosyl-binding lectin from leaves of the orchid twayblade (Listera ovata). Application to separation of α-D-mannans from α-D-glucans
    • Saito K, Komae A, Kakuta M, Van Damme EJM, Peumans WJ, Goldstein JJ, Misaki A: The alpha-mannosyl-binding lectin from leaves of the orchid twayblade (Listera ovata). Application to separation of α-D-mannans from α-D-glucans. Eur J Biochem 217: 677-681 (1993).
    • (1993) Eur J Biochem , vol.217 , pp. 677-681
    • Saito, K.1    Komae, A.2    Kakuta, M.3    Van Damme, E.J.M.4    Peumans, W.J.5    Goldstein, J.J.6    Misaki, A.7
  • 28
    • 0024286486 scopus 로고
    • Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb
    • Shibuya N, Goldstein IJ, Van Damme EJM, Peumans WJ: Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb. J Biol Chem 263: 728-734 (1988).
    • (1988) J Biol Chem , vol.263 , pp. 728-734
    • Shibuya, N.1    Goldstein, I.J.2    Van Damme, E.J.M.3    Peumans, W.J.4
  • 29
    • 0028143192 scopus 로고
    • Comparative study of the post-translational processing of the mannose-binding lectins in the bulbs of garlic (Allium sativum) and ramsons (Allium ursinum)
    • Smeets K, Van Damme EJM, Peumans WJ: Comparative study of the post-translational processing of the mannose-binding lectins in the bulbs of garlic (Allium sativum) and ramsons (Allium ursinum). Glycoconjugate J 11: 309-320 (1994).
    • (1994) Glycoconjugate J , vol.11 , pp. 309-320
    • Smeets, K.1    Van Damme, E.J.M.2    Peumans, W.J.3
  • 30
    • 0022668738 scopus 로고
    • Location of continuous antigenic determinants in the protruding regions of proteins
    • Thornton JM, Edwards MS, Taylor WR, Barlow DJ: Location of continuous antigenic determinants in the protruding regions of proteins. EMBO J 5: 409-413 (1986).
    • (1986) EMBO J , vol.5 , pp. 409-413
    • Thornton, J.M.1    Edwards, M.S.2    Taylor, W.R.3    Barlow, D.J.4
  • 32
    • 84989666997 scopus 로고
    • Lectins of members of the Amaryllidaceae are encoded by multigene families which show extensive homology
    • Van Damme EJM, Goldstein IJ, Vercammen G, Vuylsteke J, Peumans WJ: Lectins of members of the Amaryllidaceae are encoded by multigene families which show extensive homology. Physiol Plant 86: 245-252 (1992).
    • (1992) Physiol Plant , vol.86 , pp. 245-252
    • Van Damme, E.J.M.1    Goldstein, I.J.2    Vercammen, G.3    Vuylsteke, J.4    Peumans, W.J.5
  • 33
    • 0026578451 scopus 로고
    • The closely related homomeric and heterodimeric mannose-binding lectins from garlic are encoded by one-domain and two-domain lectin genes, respectively
    • Van Damme EJM, Smeets K, Torrekens S, Van Leuven F, Goldstein IJ, Peumans WJ: The closely related homomeric and heterodimeric mannose-binding lectins from garlic are encoded by one-domain and two-domain lectin genes, respectively. Eur J Biochem 206: 413-420 (1992).
    • (1992) Eur J Biochem , vol.206 , pp. 413-420
    • Van Damme, E.J.M.1    Smeets, K.2    Torrekens, S.3    Van Leuven, F.4    Goldstein, I.J.5    Peumans, W.J.6
  • 34
    • 0002241558 scopus 로고
    • Cell-free synthesis of lectins
    • Gabius H-J, Gabius S (eds), Springer-Verlag
    • Van Damme EJM, Peumans WJ: Cell-free synthesis of lectins. In Gabius H-J, Gabius S (eds), Lectins and Glycobiology, pp. 458-468, Springer-Verlag, (1993).
    • (1993) Lectins and Glycobiology , pp. 458-468
    • Van Damme, E.J.M.1    Peumans, W.J.2
  • 36
    • 0027359615 scopus 로고
    • The mannose-specific lectins from ramsons (Allium ursinum L.) are encoded by three sets of genes
    • Van Damme EJM, Smeets K, Torrekens S, Van Leuven F, Peumans WJ: The mannose-specific lectins from ramsons (Allium ursinum L.) are encoded by three sets of genes. Eur J Biochem 217: 123-129 (1993).
    • (1993) Eur J Biochem , vol.217 , pp. 123-129
    • Van Damme, E.J.M.1    Smeets, K.2    Torrekens, S.3    Van Leuven, F.4    Peumans, W.J.5
  • 37
    • 0027973161 scopus 로고
    • The monomeric and dimeric mannose-binding proteins from the Orchidaceae species Listera ovata and Epipactis helleborine: Sequence homologies and differences in biological activities
    • Van Damme EJM, Balzarini J, Smeets K, Van Leuven F, Peumans WJ: The monomeric and dimeric mannose-binding proteins from the Orchidaceae species Listera ovata and Epipactis helleborine: sequence homologies and differences in biological activities. Glycoconjugate J 11: 321-332 (1994).
    • (1994) Glycoconjugate J , vol.11 , pp. 321-332
    • Van Damme, E.J.M.1    Balzarini, J.2    Smeets, K.3    Van Leuven, F.4    Peumans, W.J.5
  • 39
    • 0028355084 scopus 로고
    • Characterization and molecular cloning of mannose-binding lectins from the Orchidaceae species Listera ovata, Epipactis helleborine and Cymbidium hybrid
    • Van Damme EJM, Smeets K, Torrekens S, Van Leuven F, Peumans WJ: Characterization and molecular cloning of mannose-binding lectins from the Orchidaceae species Listera ovata, Epipactis helleborine and Cymbidium hybrid. Eur J Biochem 221: 769-777 (1994).
    • (1994) Eur J Biochem , vol.221 , pp. 769-777
    • Van Damme, E.J.M.1    Smeets, K.2    Torrekens, S.3    Van Leuven, F.4    Peumans, W.J.5
  • 40
    • 0003116043 scopus 로고
    • The mannose binding monocot lectins and their genes
    • Pusztai AJ, Bardocz S (eds) Taylor and Francis
    • Van Damme EJM, Smeets K, Peumans WJ: The mannose binding monocot lectins and their genes. In: Pusztai AJ, Bardocz S (eds) Lectins: Biomedical Perspectives, pp. 59-80, Taylor and Francis (1995).
    • (1995) Lectins: Biomedical Perspectives , pp. 59-80
    • Van Damme, E.J.M.1    Smeets, K.2    Peumans, W.J.3
  • 41
    • 0029278698 scopus 로고
    • The major tuber storage protein of Araceae species is a lectin: Characterization and molecular cloning of the lectin from Arum maculatum L.
    • Van Damme EJM, Goossens K, Smeets K, Van Leuven F, Verhaert P, Peumans WJ: The major tuber storage protein of Araceae species is a lectin: Characterization and molecular cloning of the lectin from Arum maculatum L.. Plant Physiol 107: 1147-1158 (1995).
    • (1995) Plant Physiol , vol.107 , pp. 1147-1158
    • Van Damme, E.J.M.1    Goossens, K.2    Smeets, K.3    Van Leuven, F.4    Verhaert, P.5    Peumans, W.J.6
  • 42
    • 0029411680 scopus 로고
    • A lectin and a lectin-related protein are the two most prominent proteins in the bark of yellow wood (Cladrastis lutea)
    • Van Damme EJM, Barre A, Berner V, Rouge P, Van Leuven F, Peumans WJ: A lectin and a lectin-related protein are the two most prominent proteins in the bark of yellow wood (Cladrastis lutea). Plant Mol Biol 29: 579-598 (1995).
    • (1995) Plant Mol Biol , vol.29 , pp. 579-598
    • Van Damme, E.J.M.1    Barre, A.2    Berner, V.3    Rouge, P.4    Van Leuven, F.5    Peumans, W.J.6
  • 43
    • 0023046815 scopus 로고
    • A method for predicting signal sequence cleavage sites
    • von Heijne G: A method for predicting signal sequence cleavage sites. Nucl Acids Res 11: 4683-4690 (1986).
    • (1986) Nucl Acids Res , vol.11 , pp. 4683-4690
    • Von Heijne, G.1


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