메뉴 건너뛰기




Volumn 123, Issue 1-2, 1997, Pages 9-18

Purification of lectins from Robinia pseudoacacia L. root-tips

Author keywords

Black locust; N acetylgalactosamine; Phytohemagglutinin; Root; Symbiosis

Indexed keywords

BOVINE SERUM ALBUMIN; GLYCOPROTEIN; N ACETYLGLUCOSAMINE; OROSOMUCOID; PHYTOHEMAGGLUTININ; PLANT LECTIN;

EID: 0031588940     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(96)04562-1     Document Type: Article
Times cited : (5)

References (37)
  • 2
    • 0002199711 scopus 로고
    • Isolation, physochemical characterization and carbohydrate-binding specificity of lectins
    • I.E. Liener, N. Sharon and I.J. Goldstein (Eds), Academic Press, New York
    • [2] I.J. Goldstein and R.D. Poretz, Isolation, physochemical characterization and carbohydrate-binding specificity of lectins, in: I.E. Liener, N. Sharon and I.J. Goldstein (Eds), The Lectins: Properties, Functions and Applications in Biology and Medicine, Academic Press, New York, 1986, pp. 33-248.
    • (1986) The Lectins: Properties, Functions and Applications in Biology and Medicine , pp. 33-248
    • Goldstein, I.J.1    Poretz, R.D.2
  • 4
    • 0025222989 scopus 로고
    • Legume lectins - A large family of homologous proteins
    • [4] N. Sharon and H. Lis, Legume lectins - a large family of homologous proteins. FASEB J., 4 (1990) 3198-3208.
    • (1990) FASEB J. , vol.4 , pp. 3198-3208
    • Sharon, N.1    Lis, H.2
  • 5
    • 0001798938 scopus 로고
    • Distribution and function of plant lectins
    • I.E. Liener, N. Sharon and I.J. Goldstein (Eds), Academic Press, New York
    • [5] M.E. Etzler, Distribution and function of plant lectins, in: I.E. Liener, N. Sharon and I.J. Goldstein (Eds), The Lectins: Properties, Functions and Applications in Biology and Medicine, Academic Press, New York, 1986, pp. 371-435.
    • (1986) The Lectins: Properties, Functions and Applications in Biology and Medicine , pp. 371-435
    • Etzler, M.E.1
  • 6
    • 0002087643 scopus 로고
    • Detection of lectins in nodulated peanut and soybean plants
    • [6] B.D. Kishinevsky, I.J. Law and B.W. Strijdom, Detection of lectins in nodulated peanut and soybean plants. Planta Med., 176 (1988) 10-18.
    • (1988) Planta Med. , vol.176 , pp. 10-18
    • Kishinevsky, B.D.1    Law, I.J.2    Strijdom, B.W.3
  • 7
    • 0011237135 scopus 로고
    • Differences in properties of peanut seed lectin and purified galactose- and mannose-binding lectins from nodules of peanut
    • [7] I.J. Law, T. Haylett and B.W. Strijdom, Differences in properties of peanut seed lectin and purified galactose-and mannose-binding lectins from nodules of peanut. Planta, 176 (1988) 19-27.
    • (1988) Planta , vol.176 , pp. 19-27
    • Law, I.J.1    Haylett, T.2    Strijdom, B.W.3
  • 8
    • 0030022163 scopus 로고    scopus 로고
    • Lectin genes are expressed throughout root nodule development and during nitrogen-fixation in the Rhizobium-Medicago symbiosis
    • [8] M.A. Bauchrowitz, D. Barker and G. Truchet, Lectin genes are expressed throughout root nodule development and during nitrogen-fixation in the Rhizobium-Medicago symbiosis. Plant J., 9 (1996) 31-43.
    • (1996) Plant J. , vol.9 , pp. 31-43
    • Bauchrowitz, M.A.1    Barker, D.2    Truchet, G.3
  • 9
    • 0000739677 scopus 로고
    • The immuno-histochemical localisation of lectin in pea seeds (Pisum sativum L.)
    • [9] E. Van Driessche, G. Smets, R. Dejaegere and L. Kanarek, The immuno-histochemical localisation of lectin in pea seeds (Pisum sativum L.). Planta, 153 (1981) 287-296.
    • (1981) Planta , vol.153 , pp. 287-296
    • Van Driessche, E.1    Smets, G.2    Dejaegere, R.3    Kanarek, L.4
  • 10
    • 0011226568 scopus 로고
    • Immunocytochemical localisation of lectins in cells of Phaseolus vulgaris L. seeds
    • [10] J.F. Manen and A. Pustzai, Immunocytochemical localisation of lectins in cells of Phaseolus vulgaris L. seeds. Planta, 155 (1982) 328-334.
    • (1982) Planta , vol.155 , pp. 328-334
    • Manen, J.F.1    Pustzai, A.2
  • 11
    • 0001013533 scopus 로고
    • Seasonal fluctuations of lectins in barks of Elderberry (Sambucus nigra) and black locust (Robinia pseudoacacia)
    • [11] M. Nsimba-Lubaki and W.J. Peumans, Seasonal fluctuations of lectins in barks of Elderberry (Sambucus nigra) and Black locust (Robinia pseudoacacia). Plant Physiol., 80 (1986) 747-751.
    • (1986) Plant Physiol. , vol.80 , pp. 747-751
    • Nsimba-Lubaki, M.1    Peumans, W.J.2
  • 12
    • 0011207520 scopus 로고
    • Are bark lectins of Elderberry (Sambucus nigra) and black locust (Robinia pseudoacacia) storage proteins?
    • L.M. Shannon and M.J. Chrispeels (Eds), The American Society of Plant Physiologists, Waverly Press, Baltimore, MD
    • [12] W.J. Peumans, M. Nsimba-Lubaki, W.F. Broekaert and E.J. Van Damme, Are bark lectins of Elderberry (Sambucus nigra) and Black locust (Robinia pseudoacacia) storage proteins? in: L.M. Shannon and M.J. Chrispeels (Eds), Molecular Biology of Seed Storage Proteins and Lectins, 1986, The American Society of Plant Physiologists, Waverly Press, Baltimore, MD, pp. 53-63.
    • (1986) Molecular Biology of Seed Storage Proteins and Lectins , pp. 53-63
    • Peumans, W.J.1    Nsimba-Lubaki, M.2    Broekaert, W.F.3    Van Damme, E.J.4
  • 13
    • 0025718126 scopus 로고
    • Lectins, lectin genes and their role in plant defense
    • [13] M.J. Chrispeels and N.V. Raikhel, Lectins, lectin genes and their role in plant defense. Plant Cell, 3 (1991) 1-9.
    • (1991) Plant Cell , vol.3 , pp. 1-9
    • Chrispeels, M.J.1    Raikhel, N.V.2
  • 14
    • 0029029475 scopus 로고
    • The role of lectins in plant defense
    • [14] W.J. Peumans and E.J.M. Van Damme, The role of lectins in plant defense. Histochem. J., 27 (1995) 235-271.
    • (1995) Histochem. J. , vol.27 , pp. 235-271
    • Peumans, W.J.1    Van Damme, E.J.M.2
  • 15
    • 0011198717 scopus 로고
    • Lectins in Rhizobium-legume symbiosis
    • D.C. Kilpatrick, E. Van Driessche and T.C. Bog-Hansen (Eds), Sigma, St Louis, MO
    • [15] S.C. Ho and J.W. Kijne, Lectins in Rhizobium-legume symbiosis, in: D.C. Kilpatrick, E. Van Driessche and T.C. Bog-Hansen (Eds), Lectin Reviews, Sigma, St Louis, MO, 1991, pp. 171-181.
    • (1991) Lectin Reviews , pp. 171-181
    • Ho, S.C.1    Kijne, J.W.2
  • 16
    • 0001610633 scopus 로고
    • Root lectin as a determinant of host plant specificity in the Rhizobium-legume symbiosis
    • [16] C.L. Diaz, L.S. Melchers, P.J.J. Hooykaas, B.J.J. Lugtenberg and J.W. Kijne, Root lectin as a determinant of host plant specificity in the Rhizobium-legume symbiosis. Nature, 338 (1989) 579-581.
    • (1989) Nature , vol.338 , pp. 579-581
    • Diaz, C.L.1    Melchers, L.S.2    Hooykaas, P.J.J.3    Lugtenberg, B.J.J.4    Kijne, J.W.5
  • 17
    • 0029411320 scopus 로고
    • Sugar-binding activity of pea (Pisum sativum) lectin is essential for heterologous infection of transgenic white clover hairy roots by Rhizobium leguminosarum bv. viciae
    • [17] R.R. van Eijsden, C.L. Diaz, S. de Pater and J.W. Kijne, Sugar-binding activity of pea (Pisum sativum) lectin is essential for heterologous infection of transgenic white clover hairy roots by Rhizobium leguminosarum bv. viciae. Plant Mol. Biol., 29 (1995) 431-439.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 431-439
    • Van Eijsden, R.R.1    Diaz, C.L.2    De Pater, S.3    Kijne, J.W.4
  • 18
    • 0029190298 scopus 로고
    • Sugar-binding activity of pea lectin expressed in white clover hairy roots
    • [18] C.L. Diaz, T.J.J. Logman, H.C. Stam and J.W. Kijne, Sugar-binding activity of pea lectin expressed in white clover hairy roots. Plant Physiol., 109 (1995) 1167-1177.
    • (1995) Plant Physiol. , vol.109 , pp. 1167-1177
    • Diaz, C.L.1    Logman, T.J.J.2    Stam, H.C.3    Kijne, J.W.4
  • 19
    • 0024162546 scopus 로고
    • Black locust, the tree of agriculture
    • [19] B. Keresztezi, Black locust, the tree of agriculture. Outlook Agric., 17 (1988) 77-85.
    • (1988) Outlook Agric. , vol.17 , pp. 77-85
    • Keresztezi, B.1
  • 20
    • 0007052047 scopus 로고
    • Robinia pseudoacacia-Rhizobium symbiosis: Isolation and characterization of a fast nodulating and efficiently nitrogen fixing rhizobium strain
    • [20] M. Röhm and D. Werner, Robinia pseudoacacia-Rhizobium symbiosis: isolation and characterization of a fast nodulating and efficiently nitrogen fixing rhizobium strain. Nitrogen Fixing Tree Res. Rep., 10 (1992) 193-197.
    • (1992) Nitrogen Fixing Tree Res. Rep. , vol.10 , pp. 193-197
    • Röhm, M.1    Werner, D.2
  • 21
    • 0011250465 scopus 로고
    • Affinity chromatography of a lectin from Robinia pseudoacacia L. and demonstration of lectins in sieve-tube sap from other tree species
    • [21] C. Gietl, H. Kauss and H. Ziegler, Affinity chromatography of a lectin from Robinia pseudoacacia L. and demonstration of lectins in sieve-tube sap from other tree species. Planta, 144 (1979) 367-371.
    • (1979) Planta , vol.144 , pp. 367-371
    • Gietl, C.1    Kauss, H.2    Ziegler, H.3
  • 22
    • 0018802684 scopus 로고
    • Purification of mitogenic proteins from Hura crepitans and Robinia pseudoacacia
    • [22] A. McPherson and S. Hoover, Purification of mitogenic proteins from Hura crepitans and Robinia pseudoacacia. Biochem. Biophys. Res. Commun., 89 (1979) 713-720.
    • (1979) Biochem. Biophys. Res. Commun. , vol.89 , pp. 713-720
    • McPherson, A.1    Hoover, S.2
  • 23
    • 0023049982 scopus 로고
    • Purification and characterization of Robinia pseudoacacia seed lectins, A re-investigation
    • [23] J. Wantyghem, C. Goulut, J.P. Frénoy, E. Turpin and Y. Goussault, Purification and characterization of Robinia pseudoacacia seed lectins, A re-investigation. Biochem. J., 237 (1986) 483-489.
    • (1986) Biochem. J. , vol.237 , pp. 483-489
    • Wantyghem, J.1    Goulut, C.2    Frénoy, J.P.3    Turpin, E.4    Goussault, Y.5
  • 24
    • 0022566085 scopus 로고
    • Isolation, resolution and partial characterization of two Robinia pseudoacacia seed lectins
    • [24] G. Fleischmann and H. Rüdiger, Isolation, resolution and partial characterization of two Robinia pseudoacacia seed lectins. Biol. Chem., 367 (1986) 27-32.
    • (1986) Biol. Chem. , vol.367 , pp. 27-32
    • Fleischmann, G.1    Rüdiger, H.2
  • 25
    • 0029612354 scopus 로고
    • The seed lectins of black locust (Robinia pseudoacacia) are encoded by two genes which differ from the bark lectin genes
    • [25] E.J.M. Van Damme, A. Barre, P. Rougé, F. Van Leuven and W.J. Peumans, The seed lectins of Black locust (Robinia pseudoacacia) are encoded by two genes which differ from the bark lectin genes. Plant Mol. Biol., 29 (1995) 1197-1210.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 1197-1210
    • Van Damme, E.J.M.1    Barre, A.2    Rougé, P.3    Van Leuven, F.4    Peumans, W.J.5
  • 26
    • 0017927886 scopus 로고
    • Isolation and characterization of the lectin from black locust bark (Robinia pseudoacacia L.)
    • [26] V. Hořejší, C. Haškovec and J. Kocourek, Isolation and characterization of the lectin from Black locust bark (Robinia pseudoacacia L.). Biochim. Biophys. Acta, 532 (1978) 98-104.
    • (1978) Biochim. Biophys. Acta , vol.532 , pp. 98-104
    • Hořejší, V.1    Haškovec, C.2    Kocourek, J.3
  • 27
    • 0011176251 scopus 로고
    • The bark lectin of Robinia pseudoacacia: Purification and partial characterization
    • [27] K. Tazaki and K. Yoshida, The bark lectin of Robinia pseudoacacia: purification and partial characterization. Plant Cell Physiol., 33 (1992) 125-129.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 125-129
    • Tazaki, K.1    Yoshida, K.2
  • 28
    • 0029257506 scopus 로고
    • The bark of Robinia pseudoacacia contains a complex mixture of lectins. Characterization of the proteins and the cDNA clones
    • [28] E.J.M. Van Damme, A. Barre, K. Smeets, S. Torrekens, F. Van Leuven, P. Rougé, and W.J. Peumans, The bark of Robinia pseudoacacia contains a complex mixture of lectins. Characterization of the proteins and the cDNA clones. Plant Physiol., 107 (1995) 833-843.
    • (1995) Plant Physiol. , vol.107 , pp. 833-843
    • Van Damme, E.J.M.1    Barre, A.2    Smeets, K.3    Torrekens, S.4    Van Leuven, F.5    Rougé, P.6    Peumans, W.J.7
  • 29
    • 0028486024 scopus 로고
    • Cloning of a lectin cDNA and seasonnal changes in levels of the lectin and its mRNA in the inner bark of Robinia pseudoacacia
    • [29] K. Yoshida, K. Baba, N. Yamamoto and K. Tazaki, Cloning of a lectin cDNA and seasonnal changes in levels of the lectin and its mRNA in the inner bark of Robinia pseudoacacia. Plant Mol. Biol., 25 (1994) 845-853.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 845-853
    • Yoshida, K.1    Baba, K.2    Yamamoto, N.3    Tazaki, K.4
  • 30
    • 84986978929 scopus 로고
    • Isolation and properties of a lectin from the roots of Pisum sativum (Garden pea)
    • [30] J.A. Gatehouse and D. Boulter, Isolation and properties of a lectin from the roots of Pisum sativum (Garden pea). Physiol. Plant., 49 (1980) 437-442.
    • (1980) Physiol. Plant. , vol.49 , pp. 437-442
    • Gatehouse, J.A.1    Boulter, D.2
  • 31
    • 0003140013 scopus 로고
    • A simplified procedure for titrating hemagglutinating capacity of influenza virus and the corresponding antibody
    • [31] J.E.A. Salk, A simplified procedure for titrating hemagglutinating capacity of influenza virus and the corresponding antibody. J. Immunol., 49 (1944) 87-89.
    • (1944) J. Immunol. , vol.49 , pp. 87-89
    • Salk, J.E.A.1
  • 32
    • 0021713384 scopus 로고
    • Uptake of neoglycoproteins via membrane lectin(s) of L1210 cells evidenced by quantitative flow cytometry and drug targeting
    • [32] M. Monsigny, A.C. Roche and P. Midoux, Uptake of neoglycoproteins via membrane lectin(s) of L1210 cells evidenced by quantitative flow cytometry and drug targeting. Biol. Cell, 51 (1984) 187-196.
    • (1984) Biol. Cell , vol.51 , pp. 187-196
    • Monsigny, M.1    Roche, A.C.2    Midoux, P.3
  • 33
    • 0028174988 scopus 로고
    • Purification of an α-fucoside-binding protein from Rhizobium lupini
    • [33] J.P. Wisniewski, M. Monsigny and F.M. Delmotte, Purification of an α-fucoside-binding protein from Rhizobium lupini. Biochimie, 76 (1994) 121-128.
    • (1994) Biochimie , vol.76 , pp. 121-128
    • Wisniewski, J.P.1    Monsigny, M.2    Delmotte, F.M.3
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • [34] U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 77956989644 scopus 로고
    • Gel electrofocusing
    • [35] C.W. Wrigley, Gel electrofocusing. Methods Enzymol., 22 (1971) 559-564.
    • (1971) Methods Enzymol. , vol.22 , pp. 559-564
    • Wrigley, C.W.1
  • 36
    • 0021352340 scopus 로고
    • Improved sensitivity for detection and quantitation of glycoproteins on polyacrylamide gels
    • [36] G. Konat, H. Offner and J. Mellah, Improved sensitivity for detection and quantitation of glycoproteins on polyacrylamide gels. Experientia, 40 (1984) 303-304.
    • (1984) Experientia , vol.40 , pp. 303-304
    • Konat, G.1    Offner, H.2    Mellah, J.3
  • 37
    • 0025163557 scopus 로고
    • A facile method for the isolation and preparation of proteins and peptides for sequence analysis in the picomolar range
    • [37] J. Kurth and W. Stoffel, A facile method for the isolation and preparation of proteins and peptides for sequence analysis in the picomolar range. Biol. Chem., 371 (1990) 675-685.
    • (1990) Biol. Chem. , vol.371 , pp. 675-685
    • Kurth, J.1    Stoffel, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.