메뉴 건너뛰기




Volumn 119, Issue 2, 1996, Pages 241-252

Biofunctional membranes: An EPR study of active site structure and stability of papain non-covalently immobilized on the surface of modified poly(ether)sulfone membranes through the avidin-biotin linkage

Author keywords

Biofunctional membranes; Enzyme immobilization; EPR spectral subpopulation; Non covalent spacer; Spin labeling

Indexed keywords

AVIDIN; BENZOYLARGININE 4 NITROANILIDE; BIOTIN; CHLORIDE; PAPAIN; POLYETHER DERIVATIVE; SULFONE DERIVATIVE; THIOL PROTEINASE;

EID: 0030269426     PISSN: 03767388     EISSN: None     Source Type: Journal    
DOI: 10.1016/0376-7388(96)00124-X     Document Type: Article
Times cited : (36)

References (23)
  • 1
    • 0015881458 scopus 로고
    • An ESR study of the active site papain conformations of free and immobilized trypsin
    • [1] L.J. Berliner, S.T. Miller, U.Y. Rosa and G.P. Royer, An ESR study of the active site papain conformations of free and immobilized trypsin, Biochim. Biophys. Acta, 315 (1973) 195-199.
    • (1973) Biochim. Biophys. Acta , vol.315 , pp. 195-199
    • Berliner, L.J.1    Miller, S.T.2    Rosa, U.Y.3    Royer, G.P.4
  • 2
    • 0022557389 scopus 로고
    • Application of EPR methods in studies of immobilized enzyme systems
    • [2] G.A, Marg, G.L. Millhauser, P.S. Skerker and D.S. Clark, Application of EPR methods in studies of immobilized enzyme systems, Ann. NY Acad. Sci., 469 (1986) 253-258.
    • (1986) Ann. NY Acad. Sci. , vol.469 , pp. 253-258
    • Marg, G.A.1    Millhauser, G.L.2    Skerker, P.S.3    Clark, D.S.4
  • 3
    • 0017920266 scopus 로고
    • Spin labeling in enzymology: Spin labeled enzyme and proteins
    • [3] L.J. Berliner, Spin labeling in enzymology: spin labeled enzyme and proteins, Methods Enzymol., 49 (1978) 418-480.
    • (1978) Methods Enzymol. , vol.49 , pp. 418-480
    • Berliner, L.J.1
  • 4
    • 0020737182 scopus 로고
    • Structure-function relationships in immobilized chymotrypsin catalysis
    • [4] D.S. Clark and J.E. Bailey, Structure-function relationships in immobilized chymotrypsin catalysis, Biotechnol. Bioeng., 25 (1983) 1027-1047.
    • (1983) Biotechnol. Bioeng. , vol.25 , pp. 1027-1047
    • Clark, D.S.1    Bailey, J.E.2
  • 5
    • 0021403727 scopus 로고
    • Characterization of heterogeneous immobilized enzyme subpopulations using EPR spectroscopy
    • [5] D.S. Clark and J.E. Bailey, Characterization of heterogeneous immobilized enzyme subpopulations using EPR spectroscopy, Biotechnol. Bioeng., 26 (1984) 231-238.
    • (1984) Biotechnol. Bioeng. , vol.26 , pp. 231-238
    • Clark, D.S.1    Bailey, J.E.2
  • 6
    • 0021647323 scopus 로고
    • Kinetics and EPR spectroscopy studies of immobilized chymotrypsin deactivation
    • [6] D.S. Clark and J.E. Bailey, Kinetics and EPR spectroscopy studies of immobilized chymotrypsin deactivation, Ann. NY Acad. Sci., 434 (1984) 31-38.
    • (1984) Ann. NY Acad. Sci. , vol.434 , pp. 31-38
    • Clark, D.S.1    Bailey, J.E.2
  • 7
    • 0026816698 scopus 로고
    • Structural and enzymatic characterization of papain immobilized onto vinyl alcohol/vinyl butyral copolymer membrane
    • [7] P. Zhuang and D.A. Butterfield, Structural and enzymatic characterization of papain immobilized onto vinyl alcohol/vinyl butyral copolymer membrane, J. Membrane Sci., 66 (1992) 247-257.
    • (1992) J. Membrane Sci. , vol.66 , pp. 247-257
    • Zhuang, P.1    Butterfield, D.A.2
  • 8
    • 0026864193 scopus 로고
    • Spin labeling and kinetic studies of a membrane immobilized proteolytic enzyme
    • [8] P. Zhuang and D.A. Butterfield, Spin labeling and kinetic studies of a membrane immobilized proteolytic enzyme, Biotechnol. Prog., 8 (1992) 204-210.
    • (1992) Biotechnol. Prog. , vol.8 , pp. 204-210
    • Zhuang, P.1    Butterfield, D.A.2
  • 9
    • 0026882301 scopus 로고
    • A spin label study of immobilized enzyme spectral subpopulations
    • [9] Y. Song, G.E. Means, X. Wan and L.J. Berliner, A spin label study of immobilized enzyme spectral subpopulations, Biotechnol. Bioeng., 40 (1992) 306-312.
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 306-312
    • Song, Y.1    Means, G.E.2    Wan, X.3    Berliner, L.J.4
  • 10
    • 0028431351 scopus 로고
    • Biofunctional membranes. Part IV. Active-site structure and stability of an immobilized enzyme, papain, on modified poly(ether)sulfone membrane studied by electron paramagnetic resonance and kinetics
    • [10] D.A. Butterfield and J. Lee, S. Ganapathi and D. Bhattacharyya, Biofunctional membranes. Part IV. Active-site structure and stability of an immobilized enzyme, papain, on modified poly(ether)sulfone membrane studied by electron paramagnetic resonance and kinetics, J. Membrane Sci., 91 (1994) 47-64.
    • (1994) J. Membrane Sci. , vol.91 , pp. 47-64
    • Butterfield, D.A.1    Lee, J.2    Ganapathi, S.3    Bhattacharyya, D.4
  • 11
    • 0029379907 scopus 로고
    • Flat sheet and hollow fiber membrane bioreactors: A study of kinetics and active site conformational changes of immobilized papain including sorption studies of reaction constituents
    • [11] S. Ganapathi, D.A. Butterfield and D. Bhattacharyya, Flat sheet and hollow fiber membrane bioreactors: A study of kinetics and active site conformational changes of immobilized papain including sorption studies of reaction constituents, J. Chem. Technol. Biotechnol., 64 (1995) 157-164.
    • (1995) J. Chem. Technol. Biotechnol. , vol.64 , pp. 157-164
    • Ganapathi, S.1    Butterfield, D.A.2    Bhattacharyya, D.3
  • 12
  • 13
    • 0017138215 scopus 로고
    • Binding of chloromethyl ketone substrate analog to crystalline papain
    • [13] J. Drenth, K.H. KaIk and H.M. Swen, Binding of chloromethyl ketone substrate analog to crystalline papain, Biochemistry, 15 (1976) 3731-3738.
    • (1976) Biochemistry , vol.15 , pp. 3731-3738
    • Drenth, J.1    Kaik, K.H.2    Swen, H.M.3
  • 20
    • 0027214259 scopus 로고
    • Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 A resolution
    • [20] L. Pugliese, A. Coda, M. Malcovati and M. Bolognesi, Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 A resolution, J. Mol. Biol., 231 (1993) 698-710.
    • (1993) J. Mol. Biol. , vol.231 , pp. 698-710
    • Pugliese, L.1    Coda, A.2    Malcovati, M.3    Bolognesi, M.4
  • 21
    • 0028355868 scopus 로고
    • Active site structure and stability of thiol protease, papain, studied by electron paramagnetic resonance employing a methanethiosulfonate spin label
    • [21] D.A. Butterfield and J. Lee, Active site structure and stability of thiol protease, papain, studied by electron paramagnetic resonance employing a methanethiosulfonate spin label, Arch. Biochem. Biophys., 310(1) (1994) 167-171.
    • (1994) Arch. Biochem. Biophys. , vol.310 , Issue.1 , pp. 167-171
    • Butterfield, D.A.1    Lee, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.