메뉴 건너뛰기




Volumn 23, Issue 3, 2005, Pages 193-198

Cross-linked alginate-guar gum beads as fluidized bed affinity media for purification of jacalin

Author keywords

Alginate; Expanded bed affinity chromatography; Guar gum; Jacalin; Lectin; Protein purification

Indexed keywords

PROTEINS; PURIFICATION; REYNOLDS NUMBER;

EID: 25444483841     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2005.01.015     Document Type: Article
Times cited : (39)

References (34)
  • 3
    • 0037144158 scopus 로고    scopus 로고
    • DNA-induced inter-particle cross-linking during expanded bed adsorption chromatography. Impact on future support design
    • I. Theodossiou, and O.R. Thomas DNA-induced inter-particle cross-linking during expanded bed adsorption chromatography. Impact on future support design J. Chromatogr. A 971 2002 73 86
    • (2002) J. Chromatogr. a , vol.971 , pp. 73-86
    • Theodossiou, I.1    Thomas, O.R.2
  • 4
    • 0037473204 scopus 로고    scopus 로고
    • Capture of a recombinant protein from unclarified canola extract using streamline expanded bed anion exchange
    • Y. Bai, and C.E. Glatz Capture of a recombinant protein from unclarified canola extract using streamline expanded bed anion exchange Biotechnol. Bioeng. 81 2003 855 864
    • (2003) Biotechnol. Bioeng. , vol.81 , pp. 855-864
    • Bai, Y.1    Glatz, C.E.2
  • 5
    • 0033390884 scopus 로고    scopus 로고
    • Capture of human Fab fragments by expanded bed adsorption with a mixed mode adsorbent
    • M.B. Hansen, A. Lihme, M. Spitali, and D. King Capture of human Fab fragments by expanded bed adsorption with a mixed mode adsorbent Bioseparation 8 1999 189 193
    • (1999) Bioseparation , vol.8 , pp. 189-193
    • Hansen, M.B.1    Lihme, A.2    Spitali, M.3    King, D.4
  • 6
    • 0033388241 scopus 로고    scopus 로고
    • Comparison of batch, packed bed and expanded bed purification of A. niger cellulose using cellulose beads
    • I. Roy, A. Pai, A. Lali, and M.N. Gupta Comparison of batch, packed bed and expanded bed purification of A. niger cellulose using cellulose beads Bioseparation 8 1999 317 326
    • (1999) Bioseparation , vol.8 , pp. 317-326
    • Roy, I.1    Pai, A.2    Lali, A.3    Gupta, M.N.4
  • 7
    • 0034237335 scopus 로고    scopus 로고
    • Exploiting unusual affinity of usual polysaccharides for bioseparation of enzymes on fluidized beds
    • I. Roy, M. Sardar, and M.N. Gupta Exploiting unusual affinity of usual polysaccharides for bioseparation of enzymes on fluidized beds Enzyme Microb. Technol. 27 2000 53 65
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 53-65
    • Roy, I.1    Sardar, M.2    Gupta, M.N.3
  • 8
    • 0037716477 scopus 로고    scopus 로고
    • K-Carrageenan as a new smart macroaffinity ligand for purification of pullulanase
    • I. Roy, and M.N. Gupta k-Carrageenan as a new smart macroaffinity ligand for purification of pullulanase J. Chromatogr. A 998 2003 103 108
    • (2003) J. Chromatogr. a , vol.998 , pp. 103-108
    • Roy, I.1    Gupta, M.N.2
  • 9
    • 0142169012 scopus 로고    scopus 로고
    • Magnetic alginate microparticles for purification of α-amylase
    • M. Safarikova, I. Roy, M.N. Gupta, and I. Safarik Magnetic alginate microparticles for purification of α-amylase J. Biotechnol. 105 2003 255 260
    • (2003) J. Biotechnol. , vol.105 , pp. 255-260
    • Safarikova, M.1    Roy, I.2    Gupta, M.N.3    Safarik, I.4
  • 10
    • 0037087160 scopus 로고    scopus 로고
    • Purification of a bacterial pullulanases on a fluidized bed of calcium alginate beads
    • I. Roy, and M.N. Gupta Purification of a bacterial pullulanases on a fluidized bed of calcium alginate beads J. Chromatogr. A 950 2003 131 137
    • (2003) J. Chromatogr. a , vol.950 , pp. 131-137
    • Roy, I.1    Gupta, M.N.2
  • 11
    • 0020263478 scopus 로고
    • α-d-Galactose-specific lectin from jack fruit (Artocarpus integra) seeds
    • G.S. Kumar, P.S. Appukutan, and D.K. Basu α-d-Galactose-specific lectin from jack fruit (Artocarpus integra) seeds J. Biosci. 4 1982 257 261
    • (1982) J. Biosci. , vol.4 , pp. 257-261
    • Kumar, G.S.1    Appukutan, P.S.2    Basu, D.K.3
  • 14
    • 0018776683 scopus 로고
    • IgA contamination of IgG prepared on a protein a column
    • G.J. Van Kamp IgA contamination of IgG prepared on a protein A column J. Immunol. Methods 27 1979 301 305
    • (1979) J. Immunol. Methods , vol.27 , pp. 301-305
    • Van Kamp, G.J.1
  • 15
    • 0022626902 scopus 로고
    • Jacalin, a jack fruit lectin, precipitates IgA1 andbut not igA2 subclass on gel diffusion reaction
    • H. Kondoh, K. Kobayashi, K. Hagiwara, and T. Kajii Jacalin, a jack fruit lectin, precipitates IgA1 andbut not igA2 subclass on gel diffusion reaction J. Immunol. Methods 88 1986 171 173
    • (1986) J. Immunol. Methods , vol.88 , pp. 171-173
    • Kondoh, H.1    Kobayashi, K.2    Hagiwara, K.3    Kajii, T.4
  • 17
    • 0016564484 scopus 로고
    • The use of glutaraldehyde-treated erythrocytes for assaying the agglutinating activity of lectins
    • R.H. Turner, and I.E. Liener The use of glutaraldehyde-treated erythrocytes for assaying the agglutinating activity of lectins Anal. Biochem. 68 1975 651 653
    • (1975) Anal. Biochem. , vol.68 , pp. 651-653
    • Turner, R.H.1    Liener, I.E.2
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0001232852 scopus 로고
    • An introduction to polyacrylamide gel electrophoresis
    • D. Rickwood IRL Press Oxford
    • B.D. Hames An introduction to polyacrylamide gel electrophoresis D. Rickwood Gel Electrophoresis of Proteins: A Practical Approach 1986 IRL Press Oxford 1 86
    • (1986) Gel Electrophoresis of Proteins: A Practical Approach , pp. 1-86
    • Hames, B.D.1
  • 20
    • 0024479002 scopus 로고
    • Isolation and purification of endo-polygalacturonase by affinity chromatography in a fluidized bed reactor
    • W. Somers, K. van't Riet, H. Rozie, F. Rombouts, and J. Visser Isolation and purification of endo-polygalacturonase by affinity chromatography in a fluidized bed reactor Chem. Eng. J. 40 1989 B7 B19
    • (1989) Chem. Eng. J. , vol.40
    • Somers, W.1    Van'T Riet, K.2    Rozie, H.3    Rombouts, F.4    Visser, J.5
  • 21
    • 0033777126 scopus 로고    scopus 로고
    • Purification of alpha amylase isoenzymes from Scytalidium thermophilum on a fluidized bed of alginate beads followed by Concanavalin A-agarose column
    • I. Roy, M.S.R. Sastry, B.N. Johri, and M.N. Gupta Purification of alpha amylase isoenzymes from Scytalidium thermophilum on a fluidized bed of alginate beads followed by Concanavalin A-agarose column Protein Expr. Purif. 20 2001 162 168
    • (2001) Protein Expr. Purif. , vol.20 , pp. 162-168
    • Roy, I.1    Sastry, M.S.R.2    Johri, B.N.3    Gupta, M.N.4
  • 22
    • 0034755469 scopus 로고    scopus 로고
    • Separation of phospholipase D from peanut on a fluidized bed of crosslinked alginate beads
    • S. Sharma, I. Roy, and M.N. Gupta Separation of phospholipase D from peanut on a fluidized bed of crosslinked alginate beads Biochem. Eng. J. 8 2001 235 239
    • (2001) Biochem. Eng. J. , vol.8 , pp. 235-239
    • Sharma, S.1    Roy, I.2    Gupta, M.N.3
  • 23
  • 24
    • 0343338090 scopus 로고    scopus 로고
    • Purification of peanut lectin using guar gum as an affinity ligand
    • R. Tyagi, and M.N. Gupta Purification of peanut lectin using guar gum as an affinity ligand J. Biotechnol. 46 1996 79 83
    • (1996) J. Biotechnol. , vol.46 , pp. 79-83
    • Tyagi, R.1    Gupta, M.N.2
  • 28
    • 0001811720 scopus 로고    scopus 로고
    • Dispersion and peak shapes in chromatography
    • J.A. Jonson (Ed.), Marcel Dekker Inc., New York
    • J.A. Jonsson, Dispersion and peak shapes in chromatography. In: J.A. Jonson (Ed.), Chromatographic Theory, Basic Principles, Marcel Dekker Inc., New York, pp. 27-102.
    • Chromatographic Theory, Basic Principles , pp. 27-102
    • Jonsson, J.A.1
  • 29
    • 0021754269 scopus 로고
    • Prediction of the performance of preparative affinity chromatography
    • H.A. Chase Prediction of the performance of preparative affinity chromatography J. Chromatogr. 297 1984 179 202
    • (1984) J. Chromatogr. , vol.297 , pp. 179-202
    • Chase, H.A.1
  • 30
    • 0034688320 scopus 로고    scopus 로고
    • Facilitated downstream processing of a histidine-tagged protein from unclarified E. coli homogenates using immobilized metal affinity expanded-bed adsorption
    • R.H. Clemmitt, and H.A. Chase Facilitated downstream processing of a histidine-tagged protein from unclarified E. coli homogenates using immobilized metal affinity expanded-bed adsorption Biotechnol. Bioeng. 67 2000 206 216
    • (2000) Biotechnol. Bioeng. , vol.67 , pp. 206-216
    • Clemmitt, R.H.1    Chase, H.A.2
  • 31
    • 0006867457 scopus 로고
    • Four identical subunits in jack fruit seed agglutinin offer only two saccharide binding site
    • P.S. Appukuttan, and D.K. Basu Four identical subunits in jack fruit seed agglutinin offer only two saccharide binding site FEBS Lett. 180 1985 331 334
    • (1985) FEBS Lett. , vol.180 , pp. 331-334
    • Appukuttan, P.S.1    Basu, D.K.2
  • 32
    • 0026050394 scopus 로고
    • Preparation and X-ray characterization of four new crystal forms of Jacalin, a lectin from Artocarpus integrifolia
    • R. Banerjee, V. Dhanaraj, S.K. Mahanta, A. Surolia, and M. Vijayan Preparation and X-ray characterization of four new crystal forms of Jacalin, a lectin from Artocarpus integrifolia J. Mol. Biol. 221 1991 773 776
    • (1991) J. Mol. Biol. , vol.221 , pp. 773-776
    • Banerjee, R.1    Dhanaraj, V.2    Mahanta, S.K.3    Surolia, A.4    Vijayan, M.5
  • 33
    • 0026808536 scopus 로고
    • Thermodynamic and kinetic studies on the mechanism of binding methylumbelliferyl glycosides to Jacalin
    • D. Gupta, N.V.S.A.V. Prasad, K.D. Puri, K.L. Matta, and A. Surolia Thermodynamic and kinetic studies on the mechanism of binding methylumbelliferyl glycosides to Jacalin J. Biol. Chem. 267 1992 8908 8918
    • (1992) J. Biol. Chem. , vol.267 , pp. 8908-8918
    • Gupta, D.1    Prasad, N.V.S.A.V.2    Puri, K.D.3    Matta, K.L.4    Surolia, A.5
  • 34


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.