메뉴 건너뛰기




Volumn 37, Issue 2, 2005, Pages 205-211

Purification of Ivy, a lysozyme inhibitor from Escherichia coli, and characterisation of its specificity for various lysozymes

Author keywords

Affinity chromatography; Inhibition profile; Ivy; Lysozyme; Lysozyme inhibitor

Indexed keywords

AFFINITY CHROMATOGRAPHY; ENZYME INHIBITION; ESCHERICHIA COLI; PURIFICATION;

EID: 18844426278     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2005.03.001     Document Type: Article
Times cited : (35)

References (17)
  • 2
    • 0035947615 scopus 로고    scopus 로고
    • Escherichia coli ykfE ORFan gene encodes a potent inhibitor of c-type lysozyme
    • V. Monchois, C. Abergel, J. Sturgis, S. Jeudy, and J.M. Claverie Escherichia coli ykfE ORFan gene encodes a potent inhibitor of c-type lysozyme J Biol Chem 276 2001 18437 18441
    • (2001) J Biol Chem , vol.276 , pp. 18437-18441
    • Monchois, V.1    Abergel, C.2    Sturgis, J.3    Jeudy, S.4    Claverie, J.M.5
  • 5
    • 0036164521 scopus 로고    scopus 로고
    • Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases - Structure, function and potential for crop protection
    • O.L. Franco, D.J. Rigden, F.R. Melo, and M.F. Grossi-de-Sa Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases - structure, function and potential for crop protection Eur J Biochem 269 2002 397 412
    • (2002) Eur J Biochem , vol.269 , pp. 397-412
    • Franco, O.L.1    Rigden, D.J.2    Melo, F.R.3    Grossi-De-Sa, M.F.4
  • 7
    • 0030811909 scopus 로고    scopus 로고
    • Unexpected influence of a C-terminal-fused His-tag on the processing of an enzyme and on the kinetic and folding parameters
    • P. Ledent, C. Duez, M. Vanhove, A. Lejeune, E. Fonzé, and P. Charlier Unexpected influence of a C-terminal-fused His-tag on the processing of an enzyme and on the kinetic and folding parameters FEBS Lett 413 1997 194 196
    • (1997) FEBS Lett , vol.413 , pp. 194-196
    • Ledent, P.1    Duez, C.2    Vanhove, M.3    Lejeune, A.4    Fonzé, E.5    Charlier, P.6
  • 8
    • 0030953274 scopus 로고    scopus 로고
    • Development of a chromatographic method for the isolation and detection of hygromycin B in biological fluids
    • N.F. Campbell, L.E. Hubbard, R.S. Mazenko, and M.B. Medina Development of a chromatographic method for the isolation and detection of hygromycin B in biological fluids J Chromatogr B 692 1997 367 374
    • (1997) J Chromatogr B , vol.692 , pp. 367-374
    • Campbell, N.F.1    Hubbard, L.E.2    Mazenko, R.S.3    Medina, M.B.4
  • 9
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • M. Laemmli Cleavage of structural protein during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, M.1
  • 10
    • 0023825124 scopus 로고
    • Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels
    • J. Heukeshoven, and R. Dernick Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels Electrophoresis 9 1988 28 32
    • (1988) Electrophoresis , vol.9 , pp. 28-32
    • Heukeshoven, J.1    Dernick, R.2
  • 11
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels
    • A. Shevchenko, M. Wilm, O. Vorm, and M. Mann Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels Anal Chem 68 1996 850 858
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 12
    • 0025761294 scopus 로고
    • Second-site revertants of an active T4 lysozyme mutant restore activity by restructuring the active site cleft
    • A.R. Poteete, S. Dao-Pin, H. Nicholson, and B.W. Matthews Second-site revertants of an active T4 lysozyme mutant restore activity by restructuring the active site cleft Biochemistry 30 1991 1425 1432
    • (1991) Biochemistry , vol.30 , pp. 1425-1432
    • Poteete, A.R.1    Dao-Pin, S.2    Nicholson, H.3    Matthews, B.W.4
  • 13
    • 0028952362 scopus 로고
    • Investigations on the interactions of saccharides with the lysozyme from bacteriophage lambda
    • H.S. Duewel, E. Daub, and J.F. Honek Investigations on the interactions of saccharides with the lysozyme from bacteriophage lambda Biochim Biophys Acta 1247 1995 149 158
    • (1995) Biochim Biophys Acta , vol.1247 , pp. 149-158
    • Duewel, H.S.1    Daub, E.2    Honek, J.F.3
  • 14
    • 0035292701 scopus 로고    scopus 로고
    • Purification and characterisation of goose type lysozyme from cassowary (Casuaritus casuaritus) egg white
    • S. Thammasirirak, T. Torikata, K. Takami, K. Murata, and T. Araki Purification and characterisation of goose type lysozyme from cassowary (Casuaritus casuaritus) egg white Biosci Biotechnol Biochem 65 2001 584 592
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 584-592
    • Thammasirirak, S.1    Torikata, T.2    Takami, K.3    Murata, K.4    Araki, T.5
  • 15
    • 0021713792 scopus 로고
    • Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino-acid sequence and 3-dimensional structure during evolution
    • L.H. Weaver, M.G. Grutter, S.J. Remington, T.M. Gray, N.W. Isaacs, and B.W. Matthews Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino-acid sequence and 3-dimensional structure during evolution J Mol Evol 21 1985 97 111
    • (1985) J Mol Evol , vol.21 , pp. 97-111
    • Weaver, L.H.1    Grutter, M.G.2    Remington, S.J.3    Gray, T.M.4    Isaacs, N.W.5    Matthews, B.W.6
  • 16
    • 0032512617 scopus 로고    scopus 로고
    • Crystal structure of the lysozyme from bacteriophage lambda and its relationship with v and c-type lysozymes
    • C. Evrard, J. Fastrez, and J.-P. Declercq Crystal structure of the lysozyme from bacteriophage lambda and its relationship with v and c-type lysozymes J Mol Biol 276 1998 151 164
    • (1998) J Mol Biol , vol.276 , pp. 151-164
    • Evrard, C.1    Fastrez, J.2    Declercq, J.-P.3
  • 17
    • 0029052863 scopus 로고
    • The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes
    • A.M. Thunnissen, N.W. Isaacs, and B.W. Dijkstra The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes Proteins 22 1995 245 258
    • (1995) Proteins , vol.22 , pp. 245-258
    • Thunnissen, A.M.1    Isaacs, N.W.2    Dijkstra, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.