메뉴 건너뛰기




Volumn 4, Issue 3, 2001, Pages 32-36

Immobilization and stabilization of papain on chelating sepharose: A metal chelate regenerable carrier

Author keywords

Immobilization; Immobilized metal ion (IMI) carrier; Papain; Regeneration of matrix; Thermal stability

Indexed keywords

CHELATING AGENT; COPPER ION; METAL CHELATE; PAPAIN; SEPHAROSE;

EID: 0346691414     PISSN: 07173458     EISSN: None     Source Type: Journal    
DOI: 10.2225/vol4-issue3-fulltext-1     Document Type: Article
Times cited : (33)

References (29)
  • 1
    • 0028431351 scopus 로고
    • Bifunctional membrane Part IV. Active site structure and stability of an immobilized enzyme, papain, on modified polysulfone membranes studied by electron paramagnetic resonance and kinetics
    • Butterfield, D.A.; Lee, J.; Ganapathi, S. and Bhattacharyya, D. (1994). Bifunctional membrane Part IV. Active site structure and stability of an immobilized enzyme, papain, on modified polysulfone membranes studied by electron paramagnetic resonance and kinetics. Journal of Membrane Science 91:47-64.
    • (1994) Journal of Membrane Science , vol.91 , pp. 47-64
    • Butterfield, D.A.1    Lee, J.2    Ganapathi, S.3    Bhattacharyya, D.4
  • 2
    • 0028486177 scopus 로고
    • A general method for immobilization of glycoproteins on regenerable immobilized metal ion carriers: Application to glucose oxidase from pencillium chrysogenum and horseradish peroxidase
    • Chaga, G. (1994). A general method for immobilization of glycoproteins on regenerable immobilized metal ion carriers: Application to glucose oxidase from pencillium chrysogenum and horseradish peroxidase. Biotechnology and Applied Biochemistry 20:43-53.
    • (1994) Biotechnology and Applied Biochemistry , vol.20 , pp. 43-53
    • Chaga, G.1
  • 4
    • 0014963341 scopus 로고
    • Water-insoluble enzymes. Synthesis of a new carrier and its utilization for preparation of insoluble derivatives of papain, trypsin and subtilopeptidase A
    • Goldstein, L.; Pecht, M.; Blumberg, D.A. and Levin, Y. (1970). Water-insoluble enzymes. Synthesis of a new carrier and its utilization for preparation of insoluble derivatives of papain, trypsin and subtilopeptidase A. Biochemistry 9:2322-2333.
    • (1970) Biochemistry , vol.9 , pp. 2322-2333
    • Goldstein, L.1    Pecht, M.2    Blumberg, D.A.3    Levin, Y.4
  • 5
    • 0034565079 scopus 로고    scopus 로고
    • Assessment of synthetic peotides for hepatitis A diagnosis using biosensor technology
    • Gomara, M.J.; Ercilla, G.; Alsima, M.A. and Haro, I. (2000). Assessment of synthetic peotides for hepatitis A diagnosis using biosensor technology. Journal of Immunological Methods 246:13-24.
    • (2000) Journal of Immunological Methods , vol.246 , pp. 13-24
    • Gomara, M.J.1    Ercilla, G.2    Alsima, M.A.3    Haro, I.4
  • 6
    • 0034278090 scopus 로고    scopus 로고
    • Study on the gallic acid preparation by using immobilized tannase from Aspergillus niger
    • Guo, L.H. and Yang, S.K. (2000). Study on the gallic acid preparation by using immobilized tannase from Aspergillus niger. Shen Wu Gong Chang Xue Bao 16:614-617.
    • (2000) Shen Wu Gong Chang Xue Bao , vol.16 , pp. 614-617
    • Guo, L.H.1    Yang, S.K.2
  • 7
    • 0027529957 scopus 로고
    • Interaction of papain-digested HCA class I molecules with human alloreactive cytotoxic T lymphocytes (CTL)
    • Hausmann, R.; Zavazava, N.; Steinmann, J. and Muller-Ruchholtz, W. (1993). Interaction of papain-digested HCA class I molecules with human alloreactive cytotoxic T lymphocytes (CTL). Clinical and Experimental Immunology 91:183-188.
    • (1993) Clinical and Experimental Immunology , vol.91 , pp. 183-188
    • Hausmann, R.1    Zavazava, N.2    Steinmann, J.3    Muller-Ruchholtz, W.4
  • 8
    • 0343416805 scopus 로고    scopus 로고
    • Comparison of the properties of trypsin immobilized on 2 celite derivatives
    • Huang, X.L.; Catignani, G.L. and Swaisgood, H.E. (1997). Comparison of the properties of trypsin immobilized on 2 celite derivatives. Journal of Biotechnology 53:21-27.
    • (1997) Journal of Biotechnology , vol.53 , pp. 21-27
    • Huang, X.L.1    Catignani, G.L.2    Swaisgood, H.E.3
  • 10
    • 3242678757 scopus 로고    scopus 로고
    • Chelating Sepharose fast flow instructions
    • TK1, Uppsala, Sweden
    • Instruction bulletin of Pharmacia Biotech (1997). Chelating Sepharose fast flow instructions. TK1, Uppsala, Sweden. pp. 1-20.
    • (1997) Instruction Bulletin of Pharmacia Biotech , pp. 1-20
  • 11
    • 0020709382 scopus 로고
    • Preparation and properties of Con A cellulose immobilized glucose oxidase
    • Iqbal, J. and Saleemuddin, M. (1983a). Preparation and properties of Con A cellulose immobilized glucose oxidase. Indian Journal of Biochemistry and Biophysics 20:33-38.
    • (1983) Indian Journal of Biochemistry and Biophysics , vol.20 , pp. 33-38
    • Iqbal, J.1    Saleemuddin, M.2
  • 12
    • 0021071390 scopus 로고
    • Activity and stability of glucose oxidase and invertase immobilized on concanavalin A Sepharose: Influence of lectin concentration
    • Iqbal, J. and Saleemuddin, M. (1983b). Activity and stability of glucose oxidase and invertase immobilized on concanavalin A Sepharose: Influence of lectin concentration. Biotechnology and Bioengineering 25:3191-3195.
    • (1983) Biotechnology and Bioengineering , vol.25 , pp. 3191-3195
    • Iqbal, J.1    Saleemuddin, M.2
  • 13
    • 0014758111 scopus 로고
    • Proteases of the genus Bacillus. I Neutral proteases
    • Keay, A.J. and Wildi, B.S. (1970). Proteases of the genus Bacillus. I Neutral proteases. Biotechnology and Bioengineering 12:179-212.
    • (1970) Biotechnology and Bioengineering , vol.12 , pp. 179-212
    • Keay, A.J.1    Wildi, B.S.2
  • 14
    • 0033778711 scopus 로고    scopus 로고
    • Polyclonal antibody-mediated insolubilization and stabilization of papain
    • Khan, S.A. and Iqbal, J. (2000). Polyclonal antibody-mediated insolubilization and stabilization of papain. Biotechnology and Applied Biochemistry 32:89-94.
    • (2000) Biotechnology and Applied Biochemistry , vol.32 , pp. 89-94
    • Khan, S.A.1    Iqbal, J.2
  • 15
    • 0026190157 scopus 로고
    • Immobilization of proteases to porous chitosan beads and their catalysis for ester and peptide synthesis in organic solvents
    • Kise, H. and Hayakawa, A. (1991). Immobilization of proteases to porous chitosan beads and their catalysis for ester and peptide synthesis in organic solvents. Enzyme and Microbial Technology 13:584-588.
    • (1991) Enzyme and Microbial Technology , vol.13 , pp. 584-588
    • Kise, H.1    Hayakawa, A.2
  • 16
    • 0021711871 scopus 로고
    • Behaviour of enzyme activity in immobilized proteases
    • Kumakura, M. and Kaetsu, I. (1984). Behaviour of enzyme activity in immobilized proteases. International Journal of Biochemistry. 16:1159-1161.
    • (1984) International Journal of Biochemistry , vol.16 , pp. 1159-1161
    • Kumakura, M.1    Kaetsu, I.2
  • 17
    • 0026551730 scopus 로고
    • Comparison of lysis of bromelin and papain treated red cells in ADCC assays
    • Kumpel, B.M. and Bakacs, T. (1992). Comparison of lysis of bromelin and papain treated red cells in ADCC assays. Immunology Letters 31:237-240.
    • (1992) Immunology Letters , vol.31 , pp. 237-240
    • Kumpel, B.M.1    Bakacs, T.2
  • 18
    • 0027381577 scopus 로고
    • The contribution on intermolecular hydrogen bonding to the kinetic specificity of papain
    • Liu, S. and Hanzlik, R.P. (1993). The contribution on intermolecular hydrogen bonding to the kinetic specificity of papain. Biochemica et Biophysica Acta 1158:264-272.
    • (1993) Biochemica et Biophysica Acta , vol.1158 , pp. 264-272
    • Liu, S.1    Hanzlik, R.P.2
  • 20
    • 0027499868 scopus 로고
    • Ionization characterstics of the cys-25/His-159 and of the modulatory group of papain: Resolution of ambiguity by electronic perturbation of the quasi-2 mercaptopyridine leaving group in a new pyrimidyl disulfide reactivity probe
    • Mellor, G.W.; Thomas, E.W.; Topham, C.M. and Brocklehurst, K. (1993). Ionization characterstics of the cys-25/His-159 and of the modulatory group of papain: resolution of ambiguity by electronic perturbation of the quasi-2 mercaptopyridine leaving group in a new pyrimidyl disulfide reactivity probe. Biochemical Journal 290:289-296.
    • (1993) Biochemical Journal , vol.290 , pp. 289-296
    • Mellor, G.W.1    Thomas, E.W.2    Topham, C.M.3    Brocklehurst, K.4
  • 21
    • 0017070145 scopus 로고
    • Immobilization of enzymes by covalent binding to amine supports via cyanogens bromide activation
    • Schnapp, J. and Shalitin, Y. (1976). Immobilization of enzymes by covalent binding to amine supports via cyanogens bromide activation. Biochemical and Biophysical Research Communications 70:8-14.
    • (1976) Biochemical and Biophysical Research Communications , vol.70 , pp. 8-14
    • Schnapp, J.1    Shalitin, Y.2
  • 22
    • 0022266929 scopus 로고
    • Immobilized papain in the treatment of acute destructive lactation mastitis
    • Storozhuk, V.T.; Shamolina, I.I. and Lobova, A.B. (1985). Immobilized papain in the treatment of acute destructive lactation mastitis. Vestn. Khir Im II Grek 135:42-46.
    • (1985) Vestn. Khir. Im. II Grek. , vol.135 , pp. 42-46
    • Storozhuk, V.T.1    Shamolina, I.I.2    Lobova, A.B.3
  • 23
    • 85044700897 scopus 로고    scopus 로고
    • Immobilization of enzymes on carriers with magnetic properties: The search for optimum conditions for immobilization of alkaline phosphatase from the chicken graft
    • Surinenaite, B.R.; Bendikene, V.G. and Iuodka, B.A. (1996). Immobilization of enzymes on carriers with magnetic properties: the search for optimum conditions for immobilization of alkaline phosphatase from the chicken graft. Prikl. Biokhim. Mikrobiol. 32:609-614.
    • (1996) Prikl. Biokhim. Mikrobiol. , vol.32 , pp. 609-614
    • Surinenaite, B.R.1    Bendikene, V.G.2    Iuodka, B.A.3
  • 25
    • 0029072912 scopus 로고
    • Processing of the papain precursor. The ionization state of a conserved amino acid motif within the proregion participates in the regulation of intramolecular processing
    • Vernet, T.; Tessier, D.C.; Chatellier, J.; Plouffe, C.; Lee, T.S.; Thomas, D.Y.; Storer, A.C. and Menard, R. (1995). Processing of the papain precursor. The ionization state of a conserved amino acid motif within the proregion participates in the regulation of intramolecular processing. Journal of Biological Chemistry 27:16645-16652.
    • (1995) Journal of Biological Chemistry , vol.27 , pp. 16645-16652
    • Vernet, T.1    Tessier, D.C.2    Chatellier, J.3    Plouffe, C.4    Lee, T.S.5    Thomas, D.Y.6    Storer, A.C.7    Menard, R.8
  • 26
    • 0034489958 scopus 로고    scopus 로고
    • Immobilization of proteins on self-assembled monolayers
    • Wadu-Mesthrige, K.; Amro, N.A. and Liu, G.Y. (2000). Immobilization of proteins on self-assembled monolayers. Scanning 22:380-388.
    • (2000) Scanning , vol.22 , pp. 380-388
    • Wadu-Mesthrige, K.1    Amro, N.A.2    Liu, G.Y.3
  • 27
    • 0019880231 scopus 로고
    • Explanation of anamolous binding kinetics with a high yield immobilized enzyme system
    • Wasserman, B.P.; Jacobson, B.S. and Hultin, H.O. (1981). Explanation of anamolous binding kinetics with a high yield immobilized enzyme system. Biochemica et Biophysica Acta 657:52-57.
    • (1981) Biochemica et Biophysica Acta , vol.657 , pp. 52-57
    • Wasserman, B.P.1    Jacobson, B.S.2    Hultin, H.O.3
  • 28
    • 0027481151 scopus 로고
    • Designer enzyme and cell applications in industry and in environmental monitoring
    • Wiseman, A. (1993). Designer enzyme and cell applications in industry and in environmental monitoring. Journal of Chemical Technology and Biotechnology 56:3-13.
    • (1993) Journal of Chemical Technology and Biotechnology , vol.56 , pp. 3-13
    • Wiseman, A.1
  • 29
    • 0026864193 scopus 로고
    • Spin labeling and kinetic studies of a membrane immobilized proteolytic enzyme
    • Zhuang, P. and Butterfield, D.A. (1992). Spin labeling and kinetic studies of a membrane immobilized proteolytic enzyme. Biotechnology Progress 8:204-210.
    • (1992) Biotechnology Progress , vol.8 , pp. 204-210
    • Zhuang, P.1    Butterfield, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.