메뉴 건너뛰기




Volumn 55, Issue 3, 1997, Pages 171-179

Bioaffinity layering: A novel strategy for the immobilization of large quantities of glycoenzymes

Author keywords

Bioaffinity layering; Biosensors; Concanavalin A; Glycoenzymes; Immobilization

Indexed keywords

BATCH CELL CULTURE; BIOSENSORS; COMPOSITION; ENZYME IMMOBILIZATION; ENZYMES; GLUCOSE; PROTEINS; THERMODYNAMIC STABILITY; YEAST;

EID: 0031552592     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(97)00068-0     Document Type: Article
Times cited : (41)

References (30)
  • 1
    • 0015883619 scopus 로고
    • A novel method for the immobilization of chicken brain arylsulfatase using concanavalin A
    • Ahmad, A., Bishayee, S., Bacchawat, B.K., 1973. A novel method for the immobilization of chicken brain arylsulfatase using concanavalin A. Biochem. Biophys. Res. Commun. 53, 732-736.
    • (1973) Biochem. Biophys. Res. Commun. , vol.53 , pp. 732-736
    • Ahmad, A.1    Bishayee, S.2    Bacchawat, B.K.3
  • 3
    • 33748037939 scopus 로고
    • Enzymes of carbohydrate metabolism
    • Colowick S.P., Kaplan, N.O. (Eds.)
    • Bernfeld, P., 1955. Enzymes of carbohydrate metabolism. In: Colowick S.P., Kaplan, N.O. (Eds.), Methods Enzymol., Vol. 1, pp. 149-151.
    • (1955) Methods Enzymol. , vol.1 , pp. 149-151
    • Bernfeld, P.1
  • 4
  • 5
    • 0015979594 scopus 로고
    • Interaction between concanavalin A and brain acid hydrolases
    • Bishayee, S., Bacchawat, B.K., 1974. Interaction between concanavalin A and brain acid hydrolases. Biochim. Biophys. Acta 334, 378-387.
    • (1974) Biochim. Biophys. Acta , vol.334 , pp. 378-387
    • Bishayee, S.1    Bacchawat, B.K.2
  • 6
    • 0028486177 scopus 로고
    • A general method for the immobilization of glycoproteins on regenerable immobilized metal ion carriers: Application to glucose oxidase from pencilliun chrysogenum and horseradish peroxidase
    • Chaga, G.A., 1994. A general method for the immobilization of glycoproteins on regenerable immobilized metal ion carriers: application to glucose oxidase from pencilliun chrysogenum and horseradish peroxidase. Biotechnol. Appl. Biochem. 20, 43-53.
    • (1994) Biotechnol. Appl. Biochem. , vol.20 , pp. 43-53
    • Chaga, G.A.1
  • 7
    • 0001165802 scopus 로고
    • Purification, composition, and molecular weight of the β-galactosidase of E. coli
    • Craven, G.R., Steer, E. Jr., Anfinsen, C.B., 1965. Purification, composition, and molecular weight of the β-galactosidase of E. coli. J. Biol. Chem. 240, 2468-2477.
    • (1965) J. Biol. Chem. , vol.240 , pp. 2468-2477
    • Craven, G.R.1    Steer E., Jr.2    Anfinsen, C.B.3
  • 8
    • 0014408784 scopus 로고
    • Comparitive study of the properties of the purified internal and external invertase from yeast
    • Gascon, S., Neumann, N.P., Lampen, J.P., 1968. Comparitive study of the properties of the purified internal and external invertase from yeast. J. Biol. Chem. 243, 1573-1577.
    • (1968) J. Biol. Chem. , vol.243 , pp. 1573-1577
    • Gascon, S.1    Neumann, N.P.2    Lampen, J.P.3
  • 9
    • 0030569738 scopus 로고    scopus 로고
    • New approaches for verification of kinetic parameters of immobilized concanavalin A: Invertase preparations investigated by flow microcalorimetry
    • Gemeiner, P., Docolomansky, P., Nahalka, J., Stefuca, V., Danielsson, B., 1996. New approaches for verification of kinetic parameters of immobilized concanavalin A: Invertase preparations investigated by flow microcalorimetry. Biotechnol. Bioeng. 49, 26-35.
    • (1996) Biotechnol. Bioeng. , vol.49 , pp. 26-35
    • Gemeiner, P.1    Docolomansky, P.2    Nahalka, J.3    Stefuca, V.4    Danielsson, B.5
  • 10
    • 0017100638 scopus 로고
    • The proteolytic nature of samples of galactose oxidase. Purification of the enzyme by a simple affinity method
    • Hatton, M.W.C., Regoeczi, E., 1976. The proteolytic nature of samples of galactose oxidase. Purification of the enzyme by a simple affinity method. Biochim. Biophys. Acta 438, 339-346.
    • (1976) Biochim. Biophys. Acta , vol.438 , pp. 339-346
    • Hatton, M.W.C.1    Regoeczi, E.2
  • 11
    • 0018603869 scopus 로고
    • Immobilization of glycoenzymes through their carbohydrate chains
    • Hsiao, H., Royer, G.P., 1979. Immobilization of glycoenzymes through their carbohydrate chains. Arch. Biochem. Biophys. 198, 379-385.
    • (1979) Arch. Biochem. Biophys. , vol.198 , pp. 379-385
    • Hsiao, H.1    Royer, G.P.2
  • 12
    • 0000164274 scopus 로고
    • An inexpensive procedure for the immobilization of glycoenzymes on Sephadex G-50 using crude concanavalin A
    • Husain, Q., Saleemuddin, M., 1989. An inexpensive procedure for the immobilization of glycoenzymes on Sephadex G-50 using crude concanavalin A. Biotechnol. Appl. Biochem. 11, 508-512.
    • (1989) Biotechnol. Appl. Biochem. , vol.11 , pp. 508-512
    • Husain, Q.1    Saleemuddin, M.2
  • 13
    • 0022107819 scopus 로고
    • Entrapment of concanavalin A complexes in calcium alginate
    • Husain, Q., Iqbal, J., Saleemuddin, M., 1985. Entrapment of concanavalin A complexes in calcium alginate. Biotechnol. Bioeng. 27, 1102-1107.
    • (1985) Biotechnol. Bioeng. , vol.27 , pp. 1102-1107
    • Husain, Q.1    Iqbal, J.2    Saleemuddin, M.3
  • 14
    • 0029826815 scopus 로고    scopus 로고
    • Reversible coupling of glucoenzymes on fluoride-sensitive FET-biosensors based on lectin-glucoprotein binding
    • Köneke, R., Menzel, C., Ulber, R., Schügerl, K., Saleemuddin, M., Scheper, T., 1996. Reversible coupling of glucoenzymes on fluoride-sensitive FET-biosensors based on lectin-glucoprotein binding. Biosen. Bioelect. 11, 2, 1229-1236.
    • (1996) Biosen. Bioelect. , vol.11 , Issue.2 , pp. 1229-1236
    • Köneke, R.1    Menzel, C.2    Ulber, R.3    Schügerl, K.4    Saleemuddin, M.5    Scheper, T.6
  • 15
    • 0017151407 scopus 로고
    • Immobilized carboxypeptidase: Applications in protein chemistry
    • Liberatore, F.A., McIssac, J.E., Royer, G.P., 1976. Immobilized carboxypeptidase: applications in protein chemistry. FEBS Lett. 68, 45-48.
    • (1976) FEBS Lett. , vol.68 , pp. 45-48
    • Liberatore, F.A.1    McIssac, J.E.2    Royer, G.P.3
  • 17
    • 0023677621 scopus 로고
    • Affinity immobilization
    • Mosbach, K. (Ed.)
    • Mattiasson, B., 1988. Affinity immobilization. In: Mosbach, K. (Ed.), Methods Enzymology, Vol. 137, pp. 647-656.
    • (1988) Methods Enzymology , vol.137 , pp. 647-656
    • Mattiasson, B.1
  • 18
    • 0017861817 scopus 로고
    • An analytical flow system based on reversible immobilization of enzymes and whole cells utilizing lectin-glucoprotein interactions
    • Mattiasson, B., Borrebaeck, K., 1978. An analytical flow system based on reversible immobilization of enzymes and whole cells utilizing lectin-glucoprotein interactions. FEBS Lett. 85, 119-123.
    • (1978) FEBS Lett. , vol.85 , pp. 119-123
    • Mattiasson, B.1    Borrebaeck, K.2
  • 19
    • 0023785503 scopus 로고
    • Enzyme stabilization by immobilization
    • Mosbach, K. (Ed.)
    • Monsan, P., Combes, D., 1988. Enzyme stabilization by immobilization. In: Mosbach, K. (Ed.), Methods Enzymology, Vol. 137, pp. 584-592.
    • (1988) Methods Enzymology , vol.137 , pp. 584-592
    • Monsan, P.1    Combes, D.2
  • 20
    • 0027323972 scopus 로고
    • Properties of almond β-glucosidase immobilized on concanavalin A-Sepharose
    • Montero, M.A., Romeu, A., 1993. Properties of almond β-glucosidase immobilized on concanavalin A-Sepharose. Biochem. Mol. Biol. Int. 30, 685-689.
    • (1993) Biochem. Mol. Biol. Int. , vol.30 , pp. 685-689
    • Montero, M.A.1    Romeu, A.2
  • 21
    • 0020481202 scopus 로고
    • An experimental verification of the theory of diffusion limitation of immobilized enzyme
    • Müller, J., Zwing, T., 1982. An experimental verification of the theory of diffusion limitation of immobilized enzyme. Biochim. Biophys. Acta 705, 117-123.
    • (1982) Biochim. Biophys. Acta , vol.705 , pp. 117-123
    • Müller, J.1    Zwing, T.2
  • 22
    • 33947093960 scopus 로고
    • Immobilization of synthetically useful enzymes by condensation polymerisation
    • Pollock, A., Bangh, R.L., Adaisteinssion, O., Whilteside, G.J., 1978. Immobilization of synthetically useful enzymes by condensation polymerisation. J. Am. Chem. Soc. 100, 302-304.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 302-304
    • Pollock, A.1    Bangh, R.L.2    Adaisteinssion, O.3    Whilteside, G.J.4
  • 23
    • 0014221606 scopus 로고
    • Chemical coupling of proteins to agarose
    • Porath, J., Axen, R., Ernback, S., 1967. Chemical coupling of proteins to agarose. Nature 215, 1491-1492.
    • (1967) Nature , vol.215 , pp. 1491-1492
    • Porath, J.1    Axen, R.2    Ernback, S.3
  • 24
    • 0019482653 scopus 로고
    • Purification and characterization of a thermostable glucoamylase from the thermophilic fungus Thermomyces languginosus
    • Rao, V.B., Sastry, N.V.S., Rao, P.V.S., 1981. Purification and characterization of a thermostable glucoamylase from the thermophilic fungus Thermomyces languginosus. Biochem. J. 193, 379-387.
    • (1981) Biochem. J. , vol.193 , pp. 379-387
    • Rao, V.B.1    Sastry, N.V.S.2    Rao, P.V.S.3
  • 25
    • 0030087515 scopus 로고    scopus 로고
    • Glycoproteins: A consideration of the potential problems and their solutions with respect to purification and characterisation
    • Robertson, E.R., Kennedy, J.F., 1996. Glycoproteins: A consideration of the potential problems and their solutions with respect to purification and characterisation. Bioseparations 6, 1-15.
    • (1996) Bioseparations , vol.6 , pp. 1-15
    • Robertson, E.R.1    Kennedy, J.F.2
  • 26
    • 0026138224 scopus 로고
    • Concanavalin A: A useful ligand for glycoenzyme immobilization - A review
    • Saleemuddin, M., Husain, Q., 1991. Concanavalin A: A useful ligand for glycoenzyme immobilization - A review. Enzyme Microb. Technol. 13, 290-295.
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 290-295
    • Saleemuddin, M.1    Husain, Q.2
  • 28
    • 0021947992 scopus 로고
    • Automated determination of glucose in fermentation broths with p-hydroxybenzoic acid hydrazide
    • Schmidt, W.J., Kuhlman, W., Schügerl, K., 1985. Automated determination of glucose in fermentation broths with p-hydroxybenzoic acid hydrazide. Appl. Microbiol. Biotechnol. 21, 78-84.
    • (1985) Appl. Microbiol. Biotechnol. , vol.21 , pp. 78-84
    • Schmidt, W.J.1    Kuhlman, W.2    Schügerl, K.3
  • 29
    • 0018083709 scopus 로고
    • The involvement of salt linkages in the stabilization of baker's yeast invertase: Evidence from immobilization and stabilization studies
    • Woodward, J., Wisemann, A., 1979. The involvement of salt linkages in the stabilization of baker's yeast invertase: evidence from immobilization and stabilization studies. Biochim. Biophys. Acta 527, 8-16.
    • (1979) Biochim. Biophys. Acta , vol.527 , pp. 8-16
    • Woodward, J.1    Wisemann, A.2
  • 30
    • 0014402071 scopus 로고
    • The interaction of concanavalin A with methyl-D-glucopyranoside
    • Yariv, J., Kalb, A., Levitzki, A., 1968. The interaction of concanavalin A with methyl-D-glucopyranoside. Biochim. Biophys. Acta 165, 303-305.
    • (1968) Biochim. Biophys. Acta , vol.165 , pp. 303-305
    • Yariv, J.1    Kalb, A.2    Levitzki, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.