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Volumn 28, Issue 3, 2012, Pages 756-761

Mannose-specific lectin isolation from Canavalia ensiformis seeds by PHEMA-based cryogel

Author keywords

Con A; Cryogel; Lectin purification; Lectins; PHEMA

Indexed keywords

AFFINITY LIGANDS; BINDING CAPACITIES; BINDING STUDIES; BINDING-ELUTION CYCLE; CANAVALIA ENSIFORMIS; CARBODIIMIDES; CON A; CONCANAVALIN A; CRYOGELS; CRYOPOLYMERIZATION; LECTINS; POLY HYDROXY ETHYL METHACRYLATES; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS;

EID: 84862184066     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1552     Document Type: Article
Times cited : (20)

References (33)
  • 1
    • 11544358874 scopus 로고    scopus 로고
    • Lectins: carbohydrate-specific proteins that mediate cellular recognition
    • Lis H, Sharon N. Lectins: carbohydrate-specific proteins that mediate cellular recognition. Chem Rev. 1998; 98: 637-674.
    • (1998) Chem Rev. , vol.98 , pp. 637-674
    • Lis, H.1    Sharon, N.2
  • 3
    • 58149233859 scopus 로고    scopus 로고
    • N-acetyl-D-galactosamine-specific lectin isolation from soyflour with poly(HPMA-GMA) beads
    • Perçin I, Yavuz H, Aksöz E, Denizli A. N-acetyl-D-galactosamine-specific lectin isolation from soyflour with poly(HPMA-GMA) beads. J Appl Polym Sci. 2009; 111: 148-154.
    • (2009) J Appl Polym Sci. , vol.111 , pp. 148-154
    • Perçin, I.1    Yavuz, H.2    Aksöz, E.3    Denizli, A.4
  • 4
    • 0037164098 scopus 로고    scopus 로고
    • How proteins bind carbohydrates: lessons from legume lectins
    • Sharon N, Lis H. How proteins bind carbohydrates: lessons from legume lectins. J Agric Food Chem. 2002; 50: 6586-6591.
    • (2002) J Agric Food Chem. , vol.50 , pp. 6586-6591
    • Sharon, N.1    Lis, H.2
  • 5
    • 80855128724 scopus 로고    scopus 로고
    • The development, characterization, and demonstration of a novel strategy for purification of recombinant proteins expressed in plants
    • Tremblay R, Diao H, Huner N, Jevnikar AM, Ma S. The development, characterization, and demonstration of a novel strategy for purification of recombinant proteins expressed in plants. Transgenic Res. 2011; 20: 1357-1366.
    • (2011) Transgenic Res. , vol.20 , pp. 1357-1366
    • Tremblay, R.1    Diao, H.2    Huner, N.3    Jevnikar, A.M.4    Ma, S.5
  • 6
    • 79952438615 scopus 로고    scopus 로고
    • High-yield expression of recombinant soybean agglutinin in plants using transient and stable systems
    • Tremblay R, Feng M, Menessa R, Huner NPA, Jevnikar AM, Ma S. High-yield expression of recombinant soybean agglutinin in plants using transient and stable systems. Transgenic Res. 2011; 20: 345-356.
    • (2011) Transgenic Res. , vol.20 , pp. 345-356
    • Tremblay, R.1    Feng, M.2    Menessa, R.3    Huner, N.P.A.4    Jevnikar, A.M.5    Ma, S.6
  • 7
    • 0036703175 scopus 로고    scopus 로고
    • Plant lectins: occurrence, biochemistry, functions and applications
    • Rudiger H, Gabius HJ. Plant lectins: occurrence, biochemistry, functions and applications. Glycoconj J. 2001; 18: 589-613.
    • (2001) Glycoconj J. , vol.18 , pp. 589-613
    • Rudiger, H.1    Gabius, H.J.2
  • 8
    • 0028363373 scopus 로고
    • Isolation and characterization of an N-acetyl-D-galactosamine-binding lectin from Dutch Iris bulbs which recognizes the blood group A disaccharide (GalNAc alpha 1-3Gal)
    • Mo H, Van Damme EJ, Peumans WJ, Goldstein IJ. Isolation and characterization of an N-acetyl-D-galactosamine-binding lectin from Dutch Iris bulbs which recognizes the blood group A disaccharide (GalNAc alpha 1-3Gal). J Biol Chem. 1994; 269: 7666-7673.
    • (1994) J Biol Chem. , vol.269 , pp. 7666-7673
    • Mo, H.1    Van Damme, E.J.2    Peumans, W.J.3    Goldstein, I.J.4
  • 9
    • 0034615702 scopus 로고    scopus 로고
    • Purification and characterization of a Neu5Acα2-6Galβ1-4Glc/GlcNAc-specific lectin from the fruiting body of the polypore mushroom polyporus squamosus
    • Mo H, Winter C, Goldstein IJ. Purification and characterization of a Neu5Acα2-6Galβ1-4Glc/GlcNAc-specific lectin from the fruiting body of the polypore mushroom polyporus squamosus. J Biol Chem. 1999; 275: 10623-10629.
    • (1999) J Biol Chem. , vol.275 , pp. 10623-10629
    • Mo, H.1    Winter, C.2    Goldstein, I.J.3
  • 10
    • 4544283885 scopus 로고    scopus 로고
    • Concanavalin A immobilized affinity adsorbents for reversible use in yeast invertase adsorption
    • Yavuz H, Akgol S, Ari{dotless}ca Y, Denizli A. Concanavalin A immobilized affinity adsorbents for reversible use in yeast invertase adsorption. Macromol Biosci. 2004; 4: 674-679.
    • (2004) Macromol Biosci. , vol.4 , pp. 674-679
    • Yavuz, H.1    Akgol, S.2    Arica, Y.3    Denizli, A.4
  • 11
    • 23844550993 scopus 로고    scopus 로고
    • Antibody purification by concanavalin A affinity chromatography
    • Bereli N, Akgöl S, Yavuz H, Denizli A. Antibody purification by concanavalin A affinity chromatography. J Appl Polym Sci. 2005; 97: 1202-1208.
    • (2005) J Appl Polym Sci. , vol.97 , pp. 1202-1208
    • Bereli, N.1    Akgöl, S.2    Yavuz, H.3    Denizli, A.4
  • 13
    • 0017232340 scopus 로고
    • Structure of the concanavalin A-methyl alpha-D-mannopyranoside complex at 6-A resolution
    • Hardman KD, Ainsworth CF. Structure of the concanavalin A-methyl alpha-D-mannopyranoside complex at 6-A resolution. Biochemistry. 1976; 15: 1120-1128.
    • (1976) Biochemistry. , vol.15 , pp. 1120-1128
    • Hardman, K.D.1    Ainsworth, C.F.2
  • 14
    • 0035740634 scopus 로고    scopus 로고
    • On the role of cell surface carbohydrates and their binding proteins (lectins) in tumor metastasis
    • Gorelik E, Galili U, Raz A. On the role of cell surface carbohydrates and their binding proteins (lectins) in tumor metastasis. Cancer Metastasis Rev. 2001; 20: 245-277.
    • (2001) Cancer Metastasis Rev. , vol.20 , pp. 245-277
    • Gorelik, E.1    Galili, U.2    Raz, A.3
  • 15
    • 0242277975 scopus 로고    scopus 로고
    • Influence of postoperative complementary treatment with lectin-standardized mistletoe extract on breast cancer patients: a controlled epidemiological multicentric retrospective cohort study
    • Schumacher K, Schneider B, Reich G, Stiefel T, Stoll G, Bock PR, Hanisch J, Beuth J. Influence of postoperative complementary treatment with lectin-standardized mistletoe extract on breast cancer patients: a controlled epidemiological multicentric retrospective cohort study. Anticancer Res. 2003; 23: 5081-5087.
    • (2003) Anticancer Res. , vol.23 , pp. 5081-5087
    • Schumacher, K.1    Schneider, B.2    Reich, G.3    Stiefel, T.4    Stoll, G.5    Bock, P.R.6    Hanisch, J.7    Beuth, J.8
  • 16
    • 0037901741 scopus 로고    scopus 로고
    • The influence of dietary lectins on the cell proliferation of human breast cancer cell lines in vitro
    • Valentiner U, Fabian S, Schumacher U, Leathem AJ. The influence of dietary lectins on the cell proliferation of human breast cancer cell lines in vitro. Anticancer Res. 2003; 23: 1197-1206.
    • (2003) Anticancer Res. , vol.23 , pp. 1197-1206
    • Valentiner, U.1    Fabian, S.2    Schumacher, U.3    Leathem, A.J.4
  • 17
    • 72049120117 scopus 로고    scopus 로고
    • Plant lectins: potential antineoplastic drugs from bench to clinic
    • Liu B, Bian HJ, Bao JK. Plant lectins: potential antineoplastic drugs from bench to clinic. Cancer Lett. 2010; 287: 1-12.
    • (2010) Cancer Lett. , vol.287 , pp. 1-12
    • Liu, B.1    Bian, H.J.2    Bao, J.K.3
  • 18
    • 0000923505 scopus 로고
    • The identification of the hemagglutinin of the jack bean with concanavalin A
    • Sumner JB, Howell SE. The identification of the hemagglutinin of the jack bean with concanavalin A. J Bacteriol. 1936; 32: 227-237.
    • (1936) J Bacteriol. , vol.32 , pp. 227-237
    • Sumner, J.B.1    Howell, S.E.2
  • 19
    • 33644683787 scopus 로고    scopus 로고
    • Single step immobilized metal ion affinity precipitation/chromatography based procedures for purification of concanavalin A and Cajanus cajan mannose-specific lectin
    • Naeem A, Khan RH, Saleemuddin M. Single step immobilized metal ion affinity precipitation/chromatography based procedures for purification of concanavalin A and Cajanus cajan mannose-specific lectin. Biochemistry (Mosc). 2006; 71: 56-59.
    • (2006) Biochemistry (Mosc). , vol.71 , pp. 56-59
    • Naeem, A.1    Khan, R.H.2    Saleemuddin, M.3
  • 20
    • 84862179877 scopus 로고    scopus 로고
    • An alternate high yielding inexpensive procedure for the purification of concanavalin A
    • Khan TA, Naeem A. An alternate high yielding inexpensive procedure for the purification of concanavalin A. Biol Med. 2011; 3: 250-259.
    • (2011) Biol Med. , vol.3 , pp. 250-259
    • Khan, T.A.1    Naeem, A.2
  • 22
    • 0035865814 scopus 로고    scopus 로고
    • A new matrix for membrane affinity chromatography and its application to the purification of concanavalin A
    • Guo W, Ruckenstein E. A new matrix for membrane affinity chromatography and its application to the purification of concanavalin A. J Memb Sci. 2001; 182: 227-234.
    • (2001) J Memb Sci. , vol.182 , pp. 227-234
    • Guo, W.1    Ruckenstein, E.2
  • 23
    • 36949003722 scopus 로고    scopus 로고
    • Single step synthesis of carbohydrate monolithic capillary columns for affinity chromatography of lectins
    • Tetala KK, Chen B, Visser GM, van Beek TA. Single step synthesis of carbohydrate monolithic capillary columns for affinity chromatography of lectins. J Sep Sci. 2007; 30: 2828-2835.
    • (2007) J Sep Sci. , vol.30 , pp. 2828-2835
    • Tetala, K.K.1    Chen, B.2    Visser, G.M.3    van Beek, T.A.4
  • 25
    • 58349103736 scopus 로고    scopus 로고
    • Supermacroporous hydrophobic affinity cryogels for protein chromatography
    • Yi{dotless}lmaz F, Bereli N, Yavuz H, Denizli A. Supermacroporous hydrophobic affinity cryogels for protein chromatography. Biochem Eng J. 2009; 43: 272-279.
    • (2009) Biochem Eng J. , vol.43 , pp. 272-279
    • Yilmaz, F.1    Bereli, N.2    Yavuz, H.3    Denizli, A.4
  • 26
    • 0346034633 scopus 로고    scopus 로고
    • Direct chromatographic capture of enzyme from crude homogenate using immobilized metal affinity chromatography on a continuous supermacroporous adsorbent
    • Arvidsson P, Plieva FM, Lozinsky VI, Galaev IY, Mattiasson B. Direct chromatographic capture of enzyme from crude homogenate using immobilized metal affinity chromatography on a continuous supermacroporous adsorbent. J Chromatogr A. 2003; 986: 275-290.
    • (2003) J Chromatogr A. , vol.986 , pp. 275-290
    • Arvidsson, P.1    Plieva, F.M.2    Lozinsky, V.I.3    Galaev, I.Y.4    Mattiasson, B.5
  • 27
    • 42049086545 scopus 로고    scopus 로고
    • Protein recognition via ion-coordinated molecularly imprinted supermacroporous cryogels
    • Bereli N, Andac M, Baydemir G, Say R, Galaev IY, Denizli A. Protein recognition via ion-coordinated molecularly imprinted supermacroporous cryogels. J Chromatogr A. 2008; 1190: 18-26.
    • (2008) J Chromatogr A. , vol.1190 , pp. 18-26
    • Bereli, N.1    Andac, M.2    Baydemir, G.3    Say, R.4    Galaev, I.Y.5    Denizli, A.6
  • 28
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227: 680-685.
    • (1970) Nature. , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0034851060 scopus 로고    scopus 로고
    • Mannose-binding plant lectins: different structural scaffolds for a common sugar-recognition process
    • Barre A, Bourne Y, Van Damme EJM, Peumans WJ, Rouge P. Mannose-binding plant lectins: different structural scaffolds for a common sugar-recognition process. Biochimie. 2001; 83: 645-651.
    • (2001) Biochimie. , vol.83 , pp. 645-651
    • Barre, A.1    Bourne, Y.2    Van Damme, E.J.M.3    Peumans, W.J.4    Rouge, P.5
  • 32
    • 0016662480 scopus 로고
    • The covalent and three-dimensional structure of concanavalin a. III. Structure of the monomer and its interaction with metals and saccharides
    • Becker J, Reeke G, Wang J, Cunningham B, Edelman G. The covalent and three-dimensional structure of concanavalin a. III. Structure of the monomer and its interaction with metals and saccharides. J Biol Chem. 1975; 250: 1513-1524.
    • (1975) J Biol Chem. , vol.250 , pp. 1513-1524
    • Becker, J.1    Reeke, G.2    Wang, J.3    Cunningham, B.4    Edelman, G.5
  • 33
    • 0016662479 scopus 로고
    • The covalent and three-dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure
    • Reeke G, Becker J, Edelman, G. The covalent and three-dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure, J Biol Chem. 1975; 250: 1525-1547.
    • (1975) J Biol Chem. , vol.250 , pp. 1525-1547
    • Reeke, G.1    Becker, J.2    Edelman, G.3


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