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Volumn 6, Issue 5, 1996, Pages 283-291

Affinity precipitation of Concanavalin A with p-Aminophenyl-α-D-glucopyranoside modified Eudragit S-100: II. Kinetic studies of the formation and the dissociation of the protein-macroligand complex

Author keywords

Affinity precipitation; Concanavalin A; Dissociation of complexes; Dynamic laser light scattering; Eudragit S 100; Initial rate of complex formation

Indexed keywords

CHEMICAL MODIFICATION; COPOLYMERS; DISSOCIATION; LASER APPLICATIONS; LIGHT SCATTERING; PROTEINS; REACTION KINETICS;

EID: 0030265252     PISSN: 0923179X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (10)

References (18)
  • 1
    • 0014423864 scopus 로고
    • Protein-carbohydrate interaction. VII Physical and chemical studies on Concanavalin A, the Hemagglutinin of the Jack bean
    • Agrawal BBL and Goldstein IJ (1968) Protein-carbohydrate interaction. VII Physical and chemical studies on Concanavalin A, the Hemagglutinin of the Jack bean. Arch. Biochem. Biophys. 124: 218-229.
    • (1968) Arch. Biochem. Biophys. , vol.124 , pp. 218-229
    • Agrawal, B.B.L.1    Goldstein, I.J.2
  • 2
    • 0019217868 scopus 로고
    • Lectin-carbohydrate interactions studied by a competitive enzyme inhibition assay
    • Borrebaeck C and Mattiasson B (1980) Lectin-carbohydrate interactions studied by a competitive enzyme inhibition assay. Anal. Biochem. 107: 446-450.
    • (1980) Anal. Biochem. , vol.107 , pp. 446-450
    • Borrebaeck, C.1    Mattiasson, B.2
  • 5
    • 0029257468 scopus 로고
    • Affinity thermoprecipitation of yeast alcohol dehydrogenase through metal ion promoted binding with Eudragit Bound Cibacran blue 3GA
    • Guoqiang D, Benhura MAN, Kaul R and Mattiasson B (1995) Affinity thermoprecipitation of yeast alcohol dehydrogenase through metal ion promoted binding with Eudragit Bound Cibacran blue 3GA. Biotechnology Progress 11 (2): 187-193.
    • (1995) Biotechnology Progress , vol.11 , Issue.2 , pp. 187-193
    • Guoqiang, D.1    Benhura, M.A.N.2    Kaul, R.3    Mattiasson, B.4
  • 6
    • 0002423852 scopus 로고
    • Affinity precipitation
    • Street, G. (ed) Blackie Academic and Professional, an imprint of Chapman & Hall, Glasgow
    • Gupta MN and Mattiasson B (1994) Affinity precipitation. In: Street, G. (ed) Highly selective separations in biotechnology, (pp. 7-33) Blackie Academic and Professional, an imprint of Chapman & Hall, Glasgow.
    • (1994) Highly Selective Separations in Biotechnology , pp. 7-33
    • Gupta, M.N.1    Mattiasson, B.2
  • 8
    • 0023659492 scopus 로고
    • Separation of carbohydrates and lectins on carbohydrate-immobilized resins
    • Honda S, Suzuki S and Kakehi K (1987) Separation of carbohydrates and lectins on carbohydrate-immobilized resins. J. Chromatogr. 396: 93-100.
    • (1987) J. Chromatogr. , vol.396 , pp. 93-100
    • Honda, S.1    Suzuki, S.2    Kakehi, K.3
  • 9
    • 0029420313 scopus 로고
    • Affinity precipitation: A novel approach to protein purification
    • Irwin JA and Tipton KF (1995) Affinity precipitation: a novel approach to protein purification. Essays Biochem. 29: 137-156.
    • (1995) Essays Biochem. , vol.29 , pp. 137-156
    • Irwin, J.A.1    Tipton, K.F.2
  • 10
    • 0015622399 scopus 로고
    • Quantitative studies on the interaction of Concanavalin A, the carbohydrate-binding protein of the Jack bean, with model carbohydrate-protein conjugates
    • Iyer RN and Goldstein U (1973) Quantitative studies on the interaction of Concanavalin A, the carbohydrate-binding protein of the Jack bean, with model carbohydrate-protein conjugates. Immunochemistry 10: 313-322.
    • (1973) Immunochemistry , vol.10 , pp. 313-322
    • Iyer, R.N.1    Goldstein, U.2
  • 11
    • 0026996667 scopus 로고
    • Purification of recombinant protein A by aqueous two phase extraction integrated with affinity precipitation
    • Kamihira M, Kaul R and Mattiasson B (1992) Purification of recombinant protein A by aqueous two phase extraction integrated with affinity precipitation. Biotechnol. Bioeng. 40: 1381-1387.
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 1381-1387
    • Kamihira, M.1    Kaul, R.2    Mattiasson, B.3
  • 12
    • 0030265434 scopus 로고    scopus 로고
    • Affinity precipitation of Concanavalin A with p-aminophenyl-α-D-glucopyranoside modified Eudragit S-100. I. Initial complex formation and build-up of the precipitate
    • Linné Larsson E, Galaev IY, Lindahl L & Mattiasson B (1996) Affinity precipitation of Concanavalin A with p-aminophenyl-α-D-glucopyranoside modified Eudragit S-100. I. Initial complex formation and build-up of the precipitate. Bioseparation 6: 273-282.
    • (1996) Bioseparation , vol.6 , pp. 273-282
    • Linné Larsson, E.1    Galaev, I.Y.2    Lindahl, L.3    Mattiasson, B.4
  • 13
    • 0028010587 scopus 로고
    • Isolation of Concanavalin A by affinity precipitation
    • Linné Larsson E and Mattiasson B (1994) Isolation of Concanavalin A by affinity precipitation. Biotechnol. Techn. 8: 51-56.
    • (1994) Biotechnol. Techn. , vol.8 , pp. 51-56
    • Linné Larsson, E.1    Mattiasson, B.2
  • 14
    • 0014935999 scopus 로고
    • An examination of the topology of the saccharide binding sites of Concanavalin A and of the forces involved in complexation
    • Poretz RD and Goldstein IJ (1970) An examination of the topology of the saccharide binding sites of Concanavalin A and of the forces involved in complexation. Biochemistry 9 (14): 2890-2896.
    • (1970) Biochemistry , vol.9 , Issue.14 , pp. 2890-2896
    • Poretz, R.D.1    Goldstein, I.J.2
  • 16
    • 0028294566 scopus 로고
    • Purification of the D-lactate dehydrogenase from Leuconostoc mesenteroides ssp. cremoris using a sequential precipitation procedure
    • Shu H-C, Guoqiang D, Kaul R and Mattiasson B (1994) Purification of the D-lactate dehydrogenase from Leuconostoc mesenteroides ssp. cremoris using a sequential precipitation procedure. J. Biotechnol. 34: 1-11.
    • (1994) J. Biotechnol. , vol.34 , pp. 1-11
    • Shu, H.-C.1    Guoqiang, D.2    Kaul, R.3    Mattiasson, B.4
  • 17
    • 0014418386 scopus 로고
    • Protein-carbohydrate interaction. XX On the number of combining sites on Concanavalin A, the phytohemagglutinin of the Jack bean
    • So L, L and Goldstein IJ (1968) Protein-carbohydrate interaction. XX On the number of combining sites on Concanavalin A, the phytohemagglutinin of the Jack bean. Biochim. Biophys. Acta 165: 398-404.
    • (1968) Biochim. Biophys. Acta , vol.165 , pp. 398-404
    • So, L.L.1    Goldstein, I.J.2
  • 18
    • 0017164911 scopus 로고
    • Purification of lectins by biospecific affinity chromatography
    • Vretblad P (1976) Purification of lectins by biospecific affinity chromatography. Biochim. Biophys. Acta 434: 169-176.
    • (1976) Biochim. Biophys. Acta , vol.434 , pp. 169-176
    • Vretblad, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.