메뉴 건너뛰기




Volumn 37, Issue 5, 2004, Pages 790-802

Glutaraldehyde: Behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking

Author keywords

[No Author keywords available]

Indexed keywords

AGENTS; CONDENSATION; CROSSLINKING; ENZYMES; SOLUTIONS; THERMAL EFFECTS;

EID: 8444230519     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/04375rv01     Document Type: Review
Times cited : (1522)

References (97)
  • 1
    • 1942506926 scopus 로고
    • Cytochemistry and electron microscopy. The preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation
    • Sabatini, D.D., K. Bensch, and R.J. Barrnett. 1963. Cytochemistry and electron microscopy. The preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation. J. Cell. Biol. 17:19-58.
    • (1963) J. Cell. Biol. , vol.17 , pp. 19-58
    • Sabatini, D.D.1    Bensch, K.2    Barrnett, R.J.3
  • 2
    • 0014121820 scopus 로고
    • Purification and quantitation of glutaraldehyde and its effect on several enzyme activities in skeletal muscle
    • Anderson, P.J. 1967. Purification and quantitation of glutaraldehyde and its effect on several enzyme activities in skeletal muscle. J. Histochem. Cytochem. 15:652-661.
    • (1967) J. Histochem. Cytochem. , vol.15 , pp. 652-661
    • Anderson, P.J.1
  • 3
    • 0014166720 scopus 로고
    • The behavior of various glutaraldehydes on Sephadex G-10 and some implications for fixation
    • Hopwood, D. 1967. The behavior of various glutaraldehydes on Sephadex G-10 and some implications for fixation. Histochemie 11:289-295.
    • (1967) Histochemie , vol.11 , pp. 289-295
    • Hopwood, D.1
  • 5
    • 0242599280 scopus 로고    scopus 로고
    • Formaldehyde, formalin, paraformaldehyde and glutaraldehyde: What they are and what they do
    • 00-1
    • Kiernan, J.A. 2000. Formaldehyde, formalin, paraformaldehyde and glutaraldehyde: what they are and what they do. Microsc. Today 00-1:8-12.
    • (2000) Microsc. Today , pp. 8-12
    • Kiernan, J.A.1
  • 6
    • 0015361553 scopus 로고
    • Theoretical and practical aspects of glutaraldehyde
    • Hopwood, D. 1972. Theoretical and practical aspects of glutaraldehyde. Histochem. J. 4:267-303.
    • (1972) Histochem. J. , vol.4 , pp. 267-303
    • Hopwood, D.1
  • 9
    • 0000639866 scopus 로고
    • The enzymic behavior of carboxypeptidase-A in the solid state
    • Quiocho, F.A. and F.M. Richards. 1966. The enzymic behavior of carboxypeptidase-A in the solid state. Biochemistry. 5:4062-4076.
    • (1966) Biochemistry , vol.5 , pp. 4062-4076
    • Quiocho, F.A.1    Richards, F.M.2
  • 10
    • 0014414239 scopus 로고
    • Glutaraldehyde as a protein cross-linkage reagent
    • Richards, F.M. and J.R. Knowles. 1968. Glutaraldehyde as a protein cross-linkage reagent. J. Mol. Biol. 37:231-233.
    • (1968) J. Mol. Biol. , vol.37 , pp. 231-233
    • Richards, F.M.1    Knowles, J.R.2
  • 11
    • 0014739177 scopus 로고
    • Preparation and properties of crosslinked water-insoluble catalase
    • Schejter, A. and A. Bar-Eli. 1970. Preparation and properties of crosslinked water-insoluble catalase. Arch. Biochem. Biophys. 136:325-330.
    • (1970) Arch. Biochem. Biophys. , vol.136 , pp. 325-330
    • Schejter, A.1    Bar-Eli, A.2
  • 13
    • 0017845776 scopus 로고
    • Infiuence of the conditions of trypsin immobilization onto Spherosil on coupling efficiency
    • Monsan, P. 1978. Infiuence of the conditions of trypsin immobilization onto Spherosil on coupling efficiency. Eur. J. Appl. Microbiol. Biotechnol. 5: 1-11.
    • (1978) Eur. J. Appl. Microbiol. Biotechnol. , vol.5 , pp. 1-11
    • Monsan, P.1
  • 14
    • 0018828102 scopus 로고
    • Antimicrobial activity, uses and mechanism of action of glutaraldehyde
    • Gorman, S.P., E.M. Scott, and A.D. Russell. 1980. Antimicrobial activity, uses and mechanism of action of glutaraldehyde. J. Appl. Bacteriol. 48:161-190.
    • (1980) J. Appl. Bacteriol. , vol.48 , pp. 161-190
    • Gorman, S.P.1    Scott, E.M.2    Russell, A.D.3
  • 15
    • 0023364007 scopus 로고
    • Chemically modified collagen: A natural biomaterial for tissue replacement
    • Nimni, M.E., D. Cheung, B. Strates, M: Kodama, and K. Sheikh. 1987. Chemically modified collagen: a natural biomaterial for tissue replacement. J. Biomed. Mater. Res. 21:741-771.
    • (1987) J. Biomed. Mater. Res. , vol.21 , pp. 741-771
    • Nimni, M.E.1    Cheung, D.2    Strates, B.3    Kodama, M.4    Sheikh, K.5
  • 17
    • 0026073755 scopus 로고
    • Reaction of glutaraldehyde with amino and thiol compounds
    • Okuda, K., I. Urabe, Y. Yamada, and H. Okada. 1991. Reaction of glutaraldehyde with amino and thiol compounds. J. Ferment. Bioeng. 71:100-105.
    • (1991) J. Ferment. Bioeng. , vol.71 , pp. 100-105
    • Okuda, K.1    Urabe, I.2    Yamada, Y.3    Okada, H.4
  • 18
    • 0014425842 scopus 로고
    • The interaction of aldehydes with collagen
    • Bowes, J.H. and C.W. Cater. 1968. The interaction of aldehydes with collagen. Biochim. Biophys. Acta 168:341-352.
    • (1968) Biochim. Biophys. Acta , vol.168 , pp. 341-352
    • Bowes, J.H.1    Cater, C.W.2
  • 19
    • 0027946696 scopus 로고
    • The chemistry of enzyme and protein immobilization with glutaraldehyde
    • Walt, D.R. and V. Agayn. 1994. The chemistry of enzyme and protein immobilization with glutaraldehyde. Trends Anal. Chem. 13:425-430.
    • (1994) Trends Anal. Chem. , vol.13 , pp. 425-430
    • Walt, D.R.1    Agayn, V.2
  • 20
    • 8444248779 scopus 로고
    • Intramolecular-intermolecular polymerization of glutaraldehyde
    • Aso, C. and Y. Aito. 1962. Intramolecular-intermolecular polymerization of glutaraldehyde. Bull. Chem. Soc. Japan 35:1426.
    • (1962) Bull. Chem. Soc. Japan , vol.35 , pp. 1426
    • Aso, C.1    Aito, Y.2
  • 23
    • 0016573746 scopus 로고
    • Étude du mécanisme d'établissement des liaisons glutaraldehyde protéines
    • Monsan, P., G. Puzo, and H. Mazarguil. 1975. Étude du mécanisme d'établissement des liaisons glutaraldehyde protéines. Biochimie 57:1281-1292.
    • (1975) Biochimie , vol.57 , pp. 1281-1292
    • Monsan, P.1    Puzo, G.2    Mazarguil, H.3
  • 24
    • 0018083171 scopus 로고
    • Polyglutaraldehyde: A new reagent for coupling proteins to microspheres and for labeling cell-surface receptors
    • Rembaum, A., S. Margel, and J. Levy. 1978. Polyglutaraldehyde: a new reagent for coupling proteins to microspheres and for labeling cell-surface receptors. J. Immunol. Methods 24:239-250.
    • (1978) J. Immunol. Methods , vol.24 , pp. 239-250
    • Rembaum, A.1    Margel, S.2    Levy, J.3
  • 25
    • 0002148345 scopus 로고
    • Synthesis and characterization of poly(glutaraldehyde). A potential reagent for protein immobilization and cell separation
    • Margel, S. and A. Rembaum. 1980. Synthesis and characterization of poly(glutaraldehyde), A potential reagent for protein immobilization and cell separation. Macromolecules 13:19-24.
    • (1980) Macromolecules , vol.13 , pp. 19-24
    • Margel, S.1    Rembaum, A.2
  • 27
    • 33751500609 scopus 로고
    • Structure of a new oligomer of glutaraldehyde produced by aldol condensation reaction
    • Tashima, T., I. Masahiro, T. Kuroda, S. Yagi, and N. Terumichi. 1991. Structure of a new oligomer of glutaraldehyde produced by aldol condensation reaction. J. Org. Chem. 56:694-697.
    • (1991) J. Org. Chem. , vol.56 , pp. 694-697
    • Tashima, T.1    Masahiro, I.2    Kuroda, T.3    Yagi, S.4    Terumichi, N.5
  • 28
    • 0026558912 scopus 로고
    • The structure of glutaraldehyde in aqueous solution determined by ultraviolet absorption and light scattering
    • Kawahara, J., T. Ohmori, T. Ohkubo, S. Hattori, and M. Kawamura. 1992. The structure of glutaraldehyde in aqueous solution determined by ultraviolet absorption and light scattering. Anal. Biochem. 201:94-98.
    • (1992) Anal. Biochem. , vol.201 , pp. 94-98
    • Kawahara, J.1    Ohmori, T.2    Ohkubo, T.3    Hattori, S.4    Kawamura, M.5
  • 29
    • 0142200517 scopus 로고    scopus 로고
    • Chemical cross-linking by glutaraldehyde between amino groups: Its mechanism and effects
    • G. Swift, C.E. Carraher Jr., and C.N. Bowman (Eds.). Plenum Press, New York
    • Kawahara, J., K. Ishikawa, T. Uchimaru, and H. Takaya. 1997. Chemical cross-linking by glutaraldehyde between amino groups: its mechanism and effects, p. 119-131. In G. Swift, C.E. Carraher Jr., and C.N. Bowman (Eds.), Polymer Modification. Plenum Press, New York.
    • (1997) Polymer Modification , pp. 119-131
    • Kawahara, J.1    Ishikawa, K.2    Uchimaru, T.3    Takaya, H.4
  • 30
    • 0343141990 scopus 로고
    • Polymerization of bifunctional monomers. II. Polymerization of glutaraldehyde
    • Aso, C. and Y. Aito. 1962. Polymerization of bifunctional monomers. II. Polymerization of glutaraldehyde. Makromol. Chem. 58:195-203.
    • (1962) Makromol. Chem. , vol.58 , pp. 195-203
    • Aso, C.1    Aito, Y.2
  • 31
    • 37049139102 scopus 로고
    • Nuclear magnetic resonance measurements of equilibria involving hydration and hemiacetal formation from some carbonyl compounds
    • Hooper, D.L. 1967. Nuclear magnetic resonance measurements of equilibria involving hydration and hemiacetal formation from some carbonyl compounds. J. Chem. Soc. B: 169-170.
    • (1967) J. Chem. Soc. B , pp. 169-170
    • Hooper, D.L.1
  • 32
    • 0001257782 scopus 로고
    • Structure of aqueous glutaraldehyde
    • Whipple, E.B. and M. Ruta. 1974. Structure of aqueous glutaraldehyde. J. Org. Chem. 39:1666-1668.
    • (1974) J. Org. Chem. , vol.39 , pp. 1666-1668
    • Whipple, E.B.1    Ruta, M.2
  • 35
    • 0021346973 scopus 로고
    • The current status of fixation for electron microscopy: A review
    • Bullock, G.R. 1984. The current status of fixation for electron microscopy: a review. J. Microsc. 133:1-15.
    • (1984) J. Microsc. , vol.133 , pp. 1-15
    • Bullock, G.R.1
  • 36
    • 0017209758 scopus 로고
    • The biological uses and importance of glutaraldehyde
    • Russell, A.D. and D. Hopwood. 1976. The biological uses and importance of glutaraldehyde. Prog. Med. Chem. 13:271-301.
    • (1976) Prog. Med. Chem. , vol.13 , pp. 271-301
    • Russell, A.D.1    Hopwood, D.2
  • 37
    • 0016803785 scopus 로고
    • The reactions of glutaraldehyde with nucleic acids
    • Hopwood, D. 1975. The reactions of glutaraldehyde with nucleic acids. Histochem. J. 7:267-276.
    • (1975) Histochem. J. , vol.7 , pp. 267-276
    • Hopwood, D.1
  • 38
    • 0032783825 scopus 로고    scopus 로고
    • Metabolic stability of glutaraldehyde cross-linked peptide DNA condensates
    • Adami, R.C. and K.G. Rice. 1999. Metabolic stability of glutaraldehyde cross-linked peptide DNA condensates. J. Pharm. Sci. 88:739-746.
    • (1999) J. Pharm. Sci. , vol.88 , pp. 739-746
    • Adami, R.C.1    Rice, K.G.2
  • 40
    • 0014745457 scopus 로고
    • The reactions between glutaraldehyde and various proteins. An investigation of their kinetics
    • Hopwood, D., C.R. Callen, and M. McCabe. 1970. The reactions between glutaraldehyde and various proteins. An investigation of their kinetics. Histochem. J. 2:137-150.
    • (1970) Histochem. J. , vol.2 , pp. 137-150
    • Hopwood, D.1    Callen, C.R.2    McCabe, M.3
  • 41
    • 8444240199 scopus 로고
    • Reaction of dialdehyde with functional groups in collagen
    • Alexa, G., D. Chisalita, and G. Chirita. 1971. Reaction of dialdehyde with functional groups in collagen. Rev. Tech. Ind. Cuir. 63:5-14.
    • (1971) Rev. Tech. Ind. Cuir. , vol.63 , pp. 5-14
    • Alexa, G.1    Chisalita, D.2    Chirita, G.3
  • 42
    • 0014440127 scopus 로고
    • The cross-linking of proteins with glutaraldehyde and its use for the preparation of immunoadsorbents
    • Avrameas, S. and T. Ternynck. 1969. The cross-linking of proteins with glutaraldehyde and its use for the preparation of immunoadsorbents. Immunochem. 6:53-66.
    • (1969) Immunochem. , vol.6 , pp. 53-66
    • Avrameas, S.1    Ternynck, T.2
  • 43
    • 0016077492 scopus 로고
    • Immobilized enzymes: Analytical applications
    • Weetall, H.H. 1974. Immobilized enzymes: analytical applications. Anal. Chem. 46:602A-604A.
    • (1974) Anal. Chem. , vol.46
    • Weetall, H.H.1
  • 44
    • 0024029957 scopus 로고
    • Aldehyde-agarose gels as activated supports for immobilization- stabilization of enzymes
    • Guisán, J.M. 1988. Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes. Enzyme Microb. Technol. 10:375-382.
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 375-382
    • Guisán, J.M.1
  • 45
    • 78651149328 scopus 로고
    • Intermolecular cross-linking of a protein in the crystalline state: Carboxypeptidase A
    • Quiocho, F.A. and F.M. Richards. 1964. Intermolecular cross-linking of a protein in the crystalline state: carboxypeptidase A. Proc. Natl. Acad. Sci. USA 52:833-839.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.52 , pp. 833-839
    • Quiocho, F.A.1    Richards, F.M.2
  • 46
    • 0014447778 scopus 로고
    • Coupling of enzymes to proteins with glutaraldehyde. Use of the conjugates for the detection of antigens and antibodies
    • Avrameas, S. 1969. Coupling of enzymes to proteins with glutaraldehyde. Use of the conjugates for the detection of antigens and antibodies. Immunochemistry 6:43-52.
    • (1969) Immunochemistry , vol.6 , pp. 43-52
    • Avrameas, S.1
  • 47
    • 0017338248 scopus 로고
    • Chemical cross-linking: Reagents and problems in studies of membrane structure
    • Peters, K. and EM. Richards. 1977. Chemical cross-linking: reagents and problems in studies of membrane structure. Annu. Rev. Biochem. 46:523-551.
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 523-551
    • Peters, K.1    Richards, E.M.2
  • 48
    • 0015381563 scopus 로고
    • Advances in sterilization techniques. State of the art and recent breakthroughs
    • Boucher, R.M.G. 1972. Advances in sterilization techniques. State of the art and recent breakthroughs. Amer. J. Hosp. Pharm. 29:661-672.
    • (1972) Amer. J. Hosp. Pharm. , vol.29 , pp. 661-672
    • Boucher, R.M.G.1
  • 49
    • 0016219414 scopus 로고
    • Potentiated acid 1,5 pentanedial solution - A new chemical sterilizing and disinfecting agent
    • Boucher, R.M.G. 1974. Potentiated acid 1,5 pentanedial solution - a new chemical sterilizing and disinfecting agent. Amer. J. Hosp. Pharm. 31:546-557.
    • (1974) Amer. J. Hosp. Pharm. , vol.31 , pp. 546-557
    • Boucher, R.M.G.1
  • 50
    • 0025004712 scopus 로고
    • The effect of heating by microwave irradiation and by conventional heating on the aldehyde concentration in aqueous glutaraldehyde solutions
    • Ruijgrok, J.M., M.E. Boon, and J.R. De Wijn. 1990. The effect of heating by microwave irradiation and by conventional heating on the aldehyde concentration in aqueous glutaraldehyde solutions. Histochem. J. 22:389-393.
    • (1990) Histochem. J. , vol.22 , pp. 389-393
    • Ruijgrok, J.M.1    Boon, M.E.2    De Wijn, J.R.3
  • 51
    • 0016913414 scopus 로고
    • The nature of the cross-linking of proteins by glutaraldehyde. Part I. Interaction of glutaraldehyde with the amino-groups of 6-aminohexanoic acid and of alpha-N-acetyl-lysine
    • Hardy, P.M., A.C. Nicholls, and H.N. Rydon. 1976. The nature of the cross-linking of proteins by glutaraldehyde. Part I. Interaction of glutaraldehyde with the amino-groups of 6-aminohexanoic acid and of alpha-N-acetyl-lysine. J. Chem. Soc. Perkin Trans. 1:958-962.
    • (1976) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 958-962
    • Hardy, P.M.1    Nicholls, A.C.2    Rydon, H.N.3
  • 52
    • 37049097243 scopus 로고
    • The nature of the cross-linking of proteins by glutaraldehyde. Part 2. The formation of quaternary pyridinium compounds by the action of glutaraldehyde on proteins and the identification of a 3-(2-piperidyl)pyridinium derivative, anabilysine, as a cross-linking entity
    • Hardy, P.M., G.J. Hughes, and H.N. Rydon. 1979. The nature of the cross-linking of proteins by glutaraldehyde. Part 2. The formation of quaternary pyridinium compounds by the action of glutaraldehyde on proteins and the identification of a 3-(2-piperidyl)pyridinium derivative, anabilysine, as a cross-linking entity. J. Chem. Soc. Perkin Trans. I:2282-2288.
    • (1979) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 2282-2288
    • Hardy, P.M.1    Hughes, G.J.2    Rydon, H.N.3
  • 53
    • 0000461488 scopus 로고
    • Zum reaktionsmechanismus von glutaraldehyd mit proteinen
    • Lubig, R., P. Kusch, K. Roper, and H. Zahn. 1981. Zum reaktionsmechanismus von glutaraldehyd mit proteinen. Monatsh. Chem. 112:1313-1323.
    • (1981) Monatsh. Chem. , vol.112 , pp. 1313-1323
    • Lubig, R.1    Kusch, P.2    Roper, K.3    Zahn, H.4
  • 54
    • 0018786839 scopus 로고
    • Labelling of proteins by reductive methylation using sodium cyanoborhydride
    • Jentoft, N. and D.G. Dearborn. 1979. Labelling of proteins by reductive methylation using sodium cyanoborhydride. J. Biol. Chem. 254:4359-4365.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4359-4365
    • Jentoft, N.1    Dearborn, D.G.2
  • 56
    • 84916010496 scopus 로고
    • Bridge reactions in amino acids and fibrous proteins
    • Zahn, H. 1955. Bridge reactions in amino acids and fibrous proteins. Angew. Chem. 67:561-572.
    • (1955) Angew. Chem. , vol.67 , pp. 561-572
    • Zahn, H.1
  • 57
    • 0014735379 scopus 로고
    • The impurities in commercial glutaraldehyde and their effect on the fixation of brain
    • Robertson, E.A. and R.L. Schultz. 1970. The impurities in commercial glutaraldehyde and their effect on the fixation of brain. J. Ultrastruct. Res. 30:275-287.
    • (1970) J. Ultrastruct. Res. , vol.30 , pp. 275-287
    • Robertson, E.A.1    Schultz, R.L.2
  • 58
    • 0017272026 scopus 로고
    • Chemically aggregated enzymes
    • K. Mosbach (Ed.), Academic Press. New York
    • Broun, G.B. 1976, Chemically aggregated enzymes, p. 263-280. In K. Mosbach (Ed.), Methods in Enzymology, Academic Press. New York.
    • (1976) Methods in Enzymology , pp. 263-280
    • Broun, G.B.1
  • 61
    • 0015053879 scopus 로고
    • Cross-linking of α-chymotrypsin and other proteins by reaction with glutaraldehyde
    • Jansen, E.F., Y. Tomimatsu, and A.C. Olson. 1971. Cross-linking of α-chymotrypsin and other proteins by reaction with glutaraldehyde. Arch. Biochem. Biophys. 144:394-400.
    • (1971) Arch. Biochem. Biophys. , vol.144 , pp. 394-400
    • Jansen, E.F.1    Tomimatsu, Y.2    Olson, A.C.3
  • 62
    • 0002831721 scopus 로고
    • Physical chemical observations on the α-chymotrypsin glutaraldehyde system during formation of an insoluble derivative
    • Tomimatsu, Y., E.F. Jansen, W. Gaffield, and A.C. Olson. 1971. Physical chemical observations on the α-chymotrypsin glutaraldehyde system during formation of an insoluble derivative. J. Colloid Interface Sci. 36:51-64.
    • (1971) J. Colloid Interface Sci. , vol.36 , pp. 51-64
    • Tomimatsu, Y.1    Jansen, E.F.2    Gaffield, W.3    Olson, A.C.4
  • 63
    • 0015176980 scopus 로고
    • Modification of papain by treatment with glutaraldehyde under reducing and non-reducing conditions
    • Ottesen, M. and B. Svensson. 1971. Modification of papain by treatment with glutaraldehyde under reducing and non-reducing conditions. C.R. Trav. Lab. Carlsberg 38:171-185.
    • (1971) C.R. Trav. Lab. Carlsberg , vol.38 , pp. 171-185
    • Ottesen, M.1    Svensson, B.2
  • 64
    • 0014443048 scopus 로고
    • Properties and enzymatic activities of papain insolubilized with glutaraldehyde
    • Jansen, E.F. and A.C. Olson. 1969. Properties and enzymatic activities of papain insolubilized with glutaraldehyde. Arch. Biochem. Biophys. 129:221-227.
    • (1969) Arch. Biochem. Biophys. , vol.129 , pp. 221-227
    • Jansen, E.F.1    Olson, A.C.2
  • 65
    • 0018957044 scopus 로고
    • Studies on chemically aggregated trypsin using glutaraldehyde
    • Bano, B. and M. Saleemuddin. 1980. Studies on chemically aggregated trypsin using glutaraldehyde. Ind. J. Biochem. Biophys. 17:12-17.
    • (1980) Ind. J. Biochem. Biophys. , vol.17 , pp. 12-17
    • Bano, B.1    Saleemuddin, M.2
  • 66
    • 0005812245 scopus 로고
    • Cross-linking techniques: Application to enzyme and protein stabilization and bioconjugate preparation
    • M.E. Himmel and G. Georgiou (Eds.). American Chemical Society, Washington, DC
    • Gupta, M.N. 1993. Cross-linking techniques: application to enzyme and protein stabilization and bioconjugate preparation, p. 307-324. In M.E. Himmel and G. Georgiou (Eds.), Biocatalyst Design for Stability and Specificity. American Chemical Society, Washington, DC.
    • (1993) Biocatalyst Design for Stability and Specificity , pp. 307-324
    • Gupta, M.N.1
  • 67
    • 0031033554 scopus 로고    scopus 로고
    • Prolonged retention of cross-linked trypsin in calcium alginate microspheres
    • Chui, W.K. and L.S. Wan. 1997. Prolonged retention of cross-linked trypsin in calcium alginate microspheres. J. Microencapsulation 14:51-61.
    • (1997) J. Microencapsulation , vol.14 , pp. 51-61
    • Chui, W.K.1    Wan, L.S.2
  • 68
    • 0033570232 scopus 로고    scopus 로고
    • Protein analysis using enzymes immobilized to paramagnetic beads
    • Krogh, T.N., T. Berg, and P. Hojrup. 1999. Protein analysis using enzymes immobilized to paramagnetic beads. Anal. Biochem. 274:153-162.
    • (1999) Anal. Biochem. , vol.274 , pp. 153-162
    • Krogh, T.N.1    Berg, T.2    Hojrup, P.3
  • 69
    • 0035919535 scopus 로고    scopus 로고
    • Nonionic micellar liquid chromatography coupled to immobilized enzyme reactors
    • Tomer, S., J.G. Dorsey, and A. Berthod. 2001. Nonionic micellar liquid chromatography coupled to immobilized enzyme reactors. J. Chromatogr. A 923:7-16.
    • (2001) J. Chromatogr. A , vol.923 , pp. 7-16
    • Tomer, S.1    Dorsey, J.G.2    Berthod, A.3
  • 70
    • 0014067578 scopus 로고
    • Preparation of enzymically active, water-insoluble derivatives of trypsin
    • Habeeb, A.F. 1967. Preparation of enzymically active, water-insoluble derivatives of trypsin. Arch. Biochem. Biophys. 119:264-268.
    • (1967) Arch. Biochem. Biophys. , vol.119 , pp. 264-268
    • Habeeb, A.F.1
  • 71
    • 0015971169 scopus 로고
    • Effect of glutaraldehyde on catalase. Biochemical and cytochemical studies with beef liver catalase and rat liver peroxisomes
    • Herzog, V. and H.D. Fahimi. 1974. Effect of glutaraldehyde on catalase. Biochemical and cytochemical studies with beef liver catalase and rat liver peroxisomes. J. Cell. Biol. 60:303-311.
    • (1974) J. Cell. Biol. , vol.60 , pp. 303-311
    • Herzog, V.1    Fahimi, H.D.2
  • 72
    • 0017221823 scopus 로고
    • Assay procedures for immobilized enzymes
    • K. Mosbach (Ed.). Academic Press, New York
    • Mattiasson, B. and K. Mosbach. 1976. Assay Procedures for Immobilized Enzymes, p. 335-353. In K. Mosbach (Ed.), Methods in Enzymology. Academic Press, New York.
    • (1976) Methods in Enzymology , pp. 335-353
    • Mattiasson, B.1    Mosbach, K.2
  • 73
    • 0015957571 scopus 로고
    • Immobilized enzyme reaction stability: Attrition of the support material
    • Regan, D.L., P. Dunnill, and M.D. Lilly. 1974. Immobilized enzyme reaction stability: attrition of the support material. Biotechnol. Bioeng. XVI:333-343.
    • (1974) Biotechnol. Bioeng. , vol.16 , pp. 333-343
    • Regan, D.L.1    Dunnill, P.2    Lilly, M.D.3
  • 74
    • 3042575157 scopus 로고    scopus 로고
    • Comparison of two glutaraldehyde immobilization techniques for solid-phase tryptic peptide mapping of human hemoglobin by capillary zone electrophoresis and mass spectrometry
    • Migneault, I., C. Dartiguenave, J. Vinh, M.J. Bertrand, and K.C. Waldron. 2004. Comparison of two glutaraldehyde immobilization techniques for solid-phase tryptic peptide mapping of human hemoglobin by capillary zone electrophoresis and mass spectrometry. Electrophoresis 25:1367-1378.
    • (2004) Electrophoresis , vol.25 , pp. 1367-1378
    • Migneault, I.1    Dartiguenave, C.2    Vinh, J.3    Bertrand, M.J.4    Waldron, K.C.5
  • 76
    • 0014668090 scopus 로고
    • Enzymatically active membranes: Some properties of cellophane membranes supporting cross-linked enzymes
    • Broun, G., E. Selegny, S. Avrameas, and D. Thomas. 1969. Enzymatically active membranes: some properties of cellophane membranes supporting cross-linked enzymes. Biochim. Biophys. Acta 185:260-262.
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 260-262
    • Broun, G.1    Selegny, E.2    Avrameas, S.3    Thomas, D.4
  • 77
    • 0017872783 scopus 로고
    • The principles of enzyme stabilization. III. The effect of the length of intra-molecular cross-linkages on thermostability of enzymes
    • Torchilin, V.P., A.V. Maksimenko, V.N. Smirnov, I.V. Berezin, A.M. Klibanov, and K. Martinek. 1978. The principles of enzyme stabilization. III. The effect of the length of intra-molecular cross-linkages on thermostability of enzymes. Biochim. Biophys. Acta 522:277-283.
    • (1978) Biochim. Biophys. Acta , vol.522 , pp. 277-283
    • Torchilin, V.P.1    Maksimenko, A.V.2    Smirnov, V.N.3    Berezin, I.V.4    Klibanov, A.M.5    Martinek, K.6
  • 78
    • 0017245003 scopus 로고
    • Immobilized proteins in single crystals
    • K. Mosbach (Ed.). Academic Press, New York
    • Quiocho, F.A. 1976. Immobilized proteins in single crystals, p. 546-558. In K. Mosbach (Ed.), Methods in Enzymology. Academic Press, New York.
    • (1976) Methods in Enzymology , pp. 546-558
    • Quiocho, F.A.1
  • 79
    • 0013873779 scopus 로고
    • Water-insoluble derivatives of enzymes, antigens, and antibodies
    • Silman, L and E. Katchalski. 1966. Water-insoluble derivatives of enzymes, antigens, and antibodies. Annu. Rev. Biochem. 35:873-908.
    • (1966) Annu. Rev. Biochem. , vol.35 , pp. 873-908
    • Silman, L.1    Katchalski, E.2
  • 80
    • 0015207691 scopus 로고
    • Properties of an insoluble form of trypsin
    • Glassmeyer, C.K. and J.D. Ogle. 1971. Properties of an insoluble form of trypsin. Biochem. 10:786-792.
    • (1971) Biochem , vol.10 , pp. 786-792
    • Glassmeyer, C.K.1    Ogle, J.D.2
  • 81
    • 84913083197 scopus 로고
    • Chemical modification of bovine trypsinogen and trypsin
    • P. Desnuelle, H. Neurath and M. Ottesen (Eds.). Academic Press, New York
    • Walsh, K.A., L.L. Houston, and R.A. Kenner. 1970. Chemical modification of bovine trypsinogen and trypsin, p. 56. In P. Desnuelle, H. Neurath and M. Ottesen (Eds.), Structure-Function Relationships of Proteolytic Enzymes. Academic Press, New York.
    • (1970) Structure-Function Relationships of Proteolytic Enzymes , pp. 56
    • Walsh, K.A.1    Houston, L.L.2    Kenner, R.A.3
  • 82
    • 0013944654 scopus 로고
    • The kinetics of carboxymethylcellulose-ficin in packed beds
    • Lilly, M.D., W.E. Hornby, and E.M. Crook, 1966. The kinetics of carboxymethylcellulose-ficin in packed beds. Biochem. J. 100:718-723.
    • (1966) Biochem. J. , vol.100 , pp. 718-723
    • Lilly, M.D.1    Hornby, W.E.2    Crook, E.M.3
  • 83
    • 0015236567 scopus 로고
    • Porous glass as a solid support for immobilization or affinity chromatography of enzymes
    • Robinson, P.J., P. Dunnill, and M.D. Lilly. 1971. Porous glass as a solid support for immobilization or affinity chromatography of enzymes. Biochim. Biophys. Acta 242:659-661.
    • (1971) Biochim. Biophys. Acta , vol.242 , pp. 659-661
    • Robinson, P.J.1    Dunnill, P.2    Lilly, M.D.3
  • 84
    • 0024227826 scopus 로고
    • Studies on the immobilization of glucuronidase (Part 1). Covalent immobilization on various carriers
    • Rapatz, E., A. Travnieek, G. Fellhofer, and F. Pittner. 1988. Studies on the immobilization of glucuronidase (Part 1). Covalent immobilization on various carriers. Appl. Biochem. Biotechnol. 19:223-234.
    • (1988) Appl. Biochem. Biotechnol. , vol.19 , pp. 223-234
    • Rapatz, E.1    Travnieek, A.2    Fellhofer, G.3    Pittner, F.4
  • 85
    • 84945061190 scopus 로고
    • Immobilization of antibodies and antigens on macro solid phases. A comparison between adsorptive and covalent binding. A critical study of macro solid phases for use in immunoassay systems, Part 1
    • Wood, W.G. and A. Gadow. 1983. Immobilization of antibodies and antigens on macro solid phases. A comparison between adsorptive and covalent binding. A critical study of macro solid phases for use in immunoassay systems, Part 1. J. Clin. Chem. Clin. Biochem. 21:789-797.
    • (1983) J. Clin. Chem. Clin. Biochem. , vol.21 , pp. 789-797
    • Wood, W.G.1    Gadow, A.2
  • 86
    • 0024828631 scopus 로고
    • Immobilization of a lactase onto a magnetic support by covalent attachment to polyethyleneimine-glutaraldehyde-activated magnetite
    • Dekker, R.F. 1989. Immobilization of a lactase onto a magnetic support by covalent attachment to polyethyleneimine-glutaraldehyde-activated magnetite. Appl. Biochem. Biotechnol. 22:289-310.
    • (1989) Appl. Biochem. Biotechnol. , vol.22 , pp. 289-310
    • Dekker, R.F.1
  • 87
    • 12444268933 scopus 로고    scopus 로고
    • Oxidase enzyme immobilisation through electropolymerised films to assemble biosensors for batch and flow injection analysis
    • Badea, M., A. Curulli, and G. Palleschi. 2003. Oxidase enzyme immobilisation through electropolymerised films to assemble biosensors for batch and flow injection analysis. Biosens. Bioelectron 18:689-698.
    • (2003) Biosens. Bioelectron. , vol.18 , pp. 689-698
    • Badea, M.1    Curulli, A.2    Palleschi, G.3
  • 88
    • 0035387703 scopus 로고    scopus 로고
    • An acetylcholinesterase/choline oxidase-based amperometric biosensors as a liquid chromatography detector for acetylcholine and choline determination in brain tissue homogenates
    • Guerrieri, A. and F. Palmisano. 2001. An acetylcholinesterase/choline oxidase-based amperometric biosensors as a liquid chromatography detector for acetylcholine and choline determination in brain tissue homogenates. Anal. Chem. 73:2875-2882.
    • (2001) Anal. Chem. , vol.73 , pp. 2875-2882
    • Guerrieri, A.1    Palmisano, F.2
  • 89
    • 0347925059 scopus 로고    scopus 로고
    • Development and characterization of an immobilized enzyme reactor based on glyceraldehyde-3-phosphate dehydrogenase for on-line enzymatic studies
    • Bartolini, M., V. Andrisano, and I.W. Wainer. 2003. Development and characterization of an immobilized enzyme reactor based on glyceraldehyde-3- phosphate dehydrogenase for on-line enzymatic studies. J. Chromatogr. A 987:331-340.
    • (2003) J. Chromatogr. A , vol.987 , pp. 331-340
    • Bartolini, M.1    Andrisano, V.2    Wainer, I.W.3
  • 90
    • 0035936597 scopus 로고    scopus 로고
    • Improved determination of urinary oxalate with alkylamine glass bound barley oxalate oxidase
    • Chandran, P., M. Thakur, and C.S. Pundir. 2001. Improved determination of urinary oxalate with alkylamine glass bound barley oxalate oxidase. J. Biotechnol. 85:1-5.
    • (2001) J. Biotechnol. , vol.85 , pp. 1-5
    • Chandran, P.1    Thakur, M.2    Pundir, C.S.3
  • 91
    • 0000916487 scopus 로고
    • Cross-linked enzyme crystals as robust biocatalysts
    • St. Clair, N.L. and M.A. Navia. 1992. Cross-linked enzyme crystals as robust biocatalysts. J. Amer. Chem. Soc. 114:7314-7316.
    • (1992) J. Amer. Chem. Soc. , vol.114 , pp. 7314-7316
    • St. Clair, N.L.1    Navia, M.A.2
  • 92
    • 0034682159 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates: A simple and effective method for the immobilization of penicillin acylase
    • Cao, L., F. van Rantwijk, and R.A. Sheldon. 2000. Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase. Org. Lett. 2:1361-1364.
    • (2000) Org. Lett. , vol.2 , pp. 1361-1364
    • Cao, L.1    Van Rantwijk, F.2    Sheldon, R.A.3
  • 93
    • 0033050846 scopus 로고    scopus 로고
    • Neovascularization effect of biodegradable gelation microspheres incorporating basic fibroblast growth factor
    • Tabata, Y., S. Hijikata, M. Muniruzzaman, and Y. Ikada. 1999. Neovascularization effect of biodegradable gelation microspheres incorporating basic fibroblast growth factor. J. Biomater. Sci. Polym. Ed. 70:79-94.
    • (1999) J. Biomater. Sci. Polym. Ed. , vol.70 , pp. 79-94
    • Tabata, Y.1    Hijikata, S.2    Muniruzzaman, M.3    Ikada, Y.4
  • 94
    • 0030271509 scopus 로고    scopus 로고
    • Gelatin microspheres: Influence of preparation parameters and thermal treatment on chemico-physical and biopharmaceutical properties
    • Esposito, E., R. Cortesi, and C. Nastruzzi. 1996. Gelatin microspheres: influence of preparation parameters and thermal treatment on chemico-physical and biopharmaceutical properties. Biomater. 17:2009-2020.
    • (1996) Biomater. , vol.17 , pp. 2009-2020
    • Esposito, E.1    Cortesi, R.2    Nastruzzi, C.3
  • 95
    • 0030765941 scopus 로고    scopus 로고
    • Doxorubicin-loaded gelatin nanoparticles stabilized by glutaraldehyde: Involvement of the drug in the cross-linking process
    • Leo, E., M.A. Vandelli, R. Cameroni, and F. Forni. 1997. Doxorubicin-loaded gelatin nanoparticles stabilized by glutaraldehyde: involvement of the drug in the cross-linking process. Int. J. Pharm. 155:75-82.
    • (1997) Int. J. Pharm. , vol.155 , pp. 75-82
    • Leo, E.1    Vandelli, M.A.2    Cameroni, R.3    Forni, F.4
  • 96
    • 0026725474 scopus 로고
    • Drug encapsulation in alginate microspheres by emulsification
    • Wan, L.S.C., P.W.S. Heng, and L.W. Chan. 1992. Drug encapsulation in alginate microspheres by emulsification. J. Microencapsul. 9:309-316.
    • (1992) J. Microencapsul. , vol.9 , pp. 309-316
    • Wan, L.S.C.1    Heng, P.W.S.2    Chan, L.W.3
  • 97
    • 0033968764 scopus 로고    scopus 로고
    • Glutaraldehyde crosslinked sodium alginate beads containing liquid pesticide for soil application
    • Kulkarni, A.R., K.S. Soppimath, T.M. Aminabhavi, A.M. Dave, and M.H. Mehta. 2000. Glutaraldehyde crosslinked sodium alginate beads containing liquid pesticide for soil application. J. Control. Release 63:97-105.
    • (2000) J. Control. Release , vol.63 , pp. 97-105
    • Kulkarni, A.R.1    Soppimath, K.S.2    Aminabhavi, T.M.3    Dave, A.M.4    Mehta, M.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.