메뉴 건너뛰기




Volumn 5, Issue 11, 2005, Pages 1069-1077

Production, purification and characterisation of recombinant Fahsin, a novel antistasin-type proteinase inhibitor

Author keywords

Fahsin; Human neutrophil elastase; Inflammation; Leech; Pichia pastoris

Indexed keywords

ANTISTASIN; BDELLASTASIN; FAHSIN; FREE RADICAL; GHILANTEN; GUAMERIN; HIRUSTASIN; LEUKOCYTE ELASTASE INHIBITOR; MYELOPEROXIDASE; OXYGEN RADICAL; PIGUAMERIN; SYNTHETIC DNA; THEROSTASIN; UNCLASSIFIED DRUG;

EID: 27644439961     PISSN: 15671356     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsyr.2005.03.005     Document Type: Article
Times cited : (3)

References (33)
  • 1
    • 0029078878 scopus 로고
    • Isolation and characterization of guamerin, a new human leukocyte elastase inhibitor from Hirudo nipponia
    • H.I. Jung, S.I. Kim, K.S. Ha, C.O. Joe, and K.W. Kang Isolation and characterization of guamerin, a new human leukocyte elastase inhibitor from Hirudo nipponia J. Biol. Chem. 270 1995 13879 13884
    • (1995) J. Biol. Chem. , vol.270 , pp. 13879-13884
    • Jung, H.I.1    Kim, S.I.2    Ha, K.S.3    Joe, C.O.4    Kang, K.W.5
  • 2
    • 0000339569 scopus 로고    scopus 로고
    • Amino acid sequence of piguamerin, an antistasin-type protease inhibitor from the blood-sucking leech Hirudo nipponia
    • D.R. Kim, and K.W. Kang Amino acid sequence of piguamerin, an antistasin-type protease inhibitor from the blood-sucking leech Hirudo nipponia Eur. J. Biochem. 254 1998 692 697
    • (1998) Eur. J. Biochem. , vol.254 , pp. 692-697
    • Kim, D.R.1    Kang, K.W.2
  • 3
    • 0027972373 scopus 로고
    • Isolation and characterization of hirustasin, an antistasin-type serine-proteinase inhibitor from the medical leech Hirudo medicinalis
    • C. Sollner, R. Mentele, C. Eckerskorn, H. Fritz, and C.P. Sommerhoff Isolation and characterization of hirustasin, an antistasin-type serine-proteinase inhibitor from the medical leech Hirudo medicinalis Eur. J. Biochem. 219 1994 937 943
    • (1994) Eur. J. Biochem. , vol.219 , pp. 937-943
    • Sollner, C.1    Mentele, R.2    Eckerskorn, C.3    Fritz, H.4    Sommerhoff, C.P.5
  • 4
    • 0032054020 scopus 로고    scopus 로고
    • Bdellastasin, a serine protease inhibitor of the antistasin family from the medical leech (Hirudo medicinalis) - primary structure, expression in yeast, and characterisation of native and recombinant inhibitor
    • M. Moser, E. Auerswald, R. Mentele, C. Eckerskorn, H. Fritz, and E. Fink Bdellastasin, a serine protease inhibitor of the antistasin family from the medical leech (Hirudo medicinalis) - primary structure, expression in yeast, and characterisation of native and recombinant inhibitor Eur. J. Biochem. 253 1998 212 220
    • (1998) Eur. J. Biochem. , vol.253 , pp. 212-220
    • Moser, M.1    Auerswald, E.2    Mentele, R.3    Eckerskorn, C.4    Fritz, H.5    Fink, E.6
  • 7
    • 0031893047 scopus 로고    scopus 로고
    • Elastase inhibitor for detection and treatment of inflammation and infection
    • J. Fricker Elastase inhibitor for detection and treatment of inflammation and infection Mol. Med. Today 4 1998 5
    • (1998) Mol. Med. Today , vol.4 , pp. 5
    • Fricker, J.1
  • 8
    • 0036545373 scopus 로고    scopus 로고
    • Novel roles of protease inhibitors in infection and inflammation
    • P.S. Hiemstra Novel roles of protease inhibitors in infection and inflammation Biochem. Soc. Trans. 30 2002 116 120
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 116-120
    • Hiemstra, P.S.1
  • 9
    • 0036008393 scopus 로고    scopus 로고
    • Neutrophil elastase: path clearer, pathogen killer, or just pathologic
    • S.D. Shapiro Neutrophil elastase: path clearer, pathogen killer, or just pathologic Am. J. Respir. Cell. Mol. Biol. 26 2002 266 268
    • (2002) Am. J. Respir. Cell. Mol. Biol. , vol.26 , pp. 266-268
    • Shapiro, S.D.1
  • 10
    • 0037270522 scopus 로고    scopus 로고
    • Proteolytic host cell enzymes in gingival crevice fluid
    • V.J. Uitto, C.M. Overall, and C. McCulloch Proteolytic host cell enzymes in gingival crevice fluid Periodontology 31 2003 77 104
    • (2003) Periodontology , vol.31 , pp. 77-104
    • Uitto, V.J.1    Overall, C.M.2    McCulloch, C.3
  • 11
    • 0033485790 scopus 로고    scopus 로고
    • Serpins: an evolutionarily conserved survival strategy
    • M. Salzet, D. Vieau, and G.B. Stefano Serpins: an evolutionarily conserved survival strategy Immunol. Today 20 1999 541 544
    • (1999) Immunol. Today , vol.20 , pp. 541-544
    • Salzet, M.1    Vieau, D.2    Stefano, G.B.3
  • 12
    • 0018800894 scopus 로고
    • The oxidative inactivation of human α-1-proteinase inhibitor. Further evidence for methionine at the reactive center
    • D. Johnson, and J. Travis The oxidative inactivation of human α-1-proteinase inhibitor. Further evidence for methionine at the reactive center J. Biol. Chem. 254 1979 4022 4026
    • (1979) J. Biol. Chem. , vol.254 , pp. 4022-4026
    • Johnson, D.1    Travis, J.2
  • 13
    • 0024501812 scopus 로고
    • Inhibition of neutrophil elastase by α-1-proteinase inhibitor oxidized by activated neutrophils
    • M. Padrines, M. Schneider-Pozzer, and J.G. Bieth Inhibition of neutrophil elastase by α-1-proteinase inhibitor oxidized by activated neutrophils Am. Rev. Respir. Dis. 139 1989 783 790
    • (1989) Am. Rev. Respir. Dis. , vol.139 , pp. 783-790
    • Padrines, M.1    Schneider-Pozzer, M.2    Bieth, J.G.3
  • 14
    • 0037789214 scopus 로고    scopus 로고
    • Inhibition of proteinase 3 by α1-antitrypsin in vitro predicts very fast inhibition in vivo
    • J. Duranton, and J.G. Bieth Inhibition of proteinase 3 by α1-antitrypsin in vitro predicts very fast inhibition in vivo Am. J. Respir. Cell. Mol. Biol. 29 2003 57 61
    • (2003) Am. J. Respir. Cell. Mol. Biol. , vol.29 , pp. 57-61
    • Duranton, J.1    Bieth, J.G.2
  • 15
    • 27644506236 scopus 로고    scopus 로고
    • A novel family of protease inhibitors and other biologically active substances. Pat. Appl. WO 9613585.
    • Voerman, G. (1996) A novel family of protease inhibitors and other biologically active substances. Pat. Appl. WO 9613585.
    • (1996)
    • Voerman, G.1
  • 16
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • S.N. Ho, H.D. Hunt, R.M. Horton, J.K. Pullen, and L.R. Pease Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77 1989 51 59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 18
    • 0025974216 scopus 로고
    • High-efficiency transformation of yeast by electroporation
    • D.M. Becker, and L. Guarente High-efficiency transformation of yeast by electroporation Methods Enzymol. 194 1991 182 187
    • (1991) Methods Enzymol. , vol.194 , pp. 182-187
    • Becker, D.M.1    Guarente, L.2
  • 19
    • 0033844101 scopus 로고    scopus 로고
    • Production and purification of the heavy chain fragment C of botulinum neurotoxin, serotype A, expressed in the methylotrophic yeast Pichia pastoris
    • K.J. Potter, W. Zhang, L.A. Smith, and M.M. Meagher Production and purification of the heavy chain fragment C of botulinum neurotoxin, serotype A, expressed in the methylotrophic yeast Pichia pastoris Protein Expr. Purif. 19 2000 393 402
    • (2000) Protein Expr. Purif. , vol.19 , pp. 393-402
    • Potter, K.J.1    Zhang, W.2    Smith, L.A.3    Meagher, M.M.4
  • 21
    • 0030778083 scopus 로고    scopus 로고
    • Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase
    • H.R. Ellis, and L.B. Poole Novel application of 7-chloro-4-nitrobenzo-2- oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase Biochemistry 36 1997 15013 15018
    • (1997) Biochemistry , vol.36 , pp. 15013-15018
    • Ellis, H.R.1    Poole, L.B.2
  • 22
    • 0028064657 scopus 로고
    • Oxidized mucus proteinase inhibitor: a fairly potent neutrophil elastase inhibitor
    • C. Boudier, and J.G. Bieth Oxidized mucus proteinase inhibitor: a fairly potent neutrophil elastase inhibitor Biochem. J. 303 1994 61 68
    • (1994) Biochem. J. , vol.303 , pp. 61-68
    • Boudier, C.1    Bieth, J.G.2
  • 23
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • M. Dixon The determination of enzyme inhibitor constants Biochem. J. 55 1953 170 171
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 25
    • 0024445042 scopus 로고
    • Antistasin, a leech-derived inhibitor of factor Xa. Kinetic analysis of enzyme inhibition and identification of the reactive site
    • C. Dunwiddie, N.A. Thornberry, H.G. Bull, M. Sardana, P.A. Friedman, J.W. Jacobs, and E. Simpson Antistasin, a leech-derived inhibitor of factor Xa. Kinetic analysis of enzyme inhibition and identification of the reactive site J. Biol. Chem. 264 1989 16694 16699
    • (1989) J. Biol. Chem. , vol.264 , pp. 16694-16699
    • Dunwiddie, C.1    Thornberry, N.A.2    Bull, H.G.3    Sardana, M.4    Friedman, P.A.5    Jacobs, J.W.6    Simpson, E.7
  • 26
    • 0025117387 scopus 로고
    • Amino acid sequence of ghilanten: anticoagulant-antimetastatic principle of the South American leech, Haementeria ghilianii
    • D.T. Blankenship, R.G. Brankamp, G.D. Manley, and A.D. Cardin Amino acid sequence of ghilanten: anticoagulant-antimetastatic principle of the South American leech, Haementeria ghilianii Biochem. Biophys. Res. Commun. 166 1990 1384 1389
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 1384-1389
    • Blankenship, D.T.1    Brankamp, R.G.2    Manley, G.D.3    Cardin, A.D.4
  • 28
    • 0036800809 scopus 로고    scopus 로고
    • Hirudin as alternative anticoagulant - a historical review
    • F. Markwardt Hirudin as alternative anticoagulant - a historical review Semin. Thromb. Hemost. 28 2002 405 414
    • (2002) Semin. Thromb. Hemost. , vol.28 , pp. 405-414
    • Markwardt, F.1
  • 29
    • 0030475733 scopus 로고    scopus 로고
    • Production and purification of recombinant hirudin expressed in the methylotrophic yeast Pichia pastoris
    • S.A. Rosenfeld, D. Nadeau, J. Tirado, G.F. Hollis, R.M. Knabb, and S. Jia Production and purification of recombinant hirudin expressed in the methylotrophic yeast Pichia pastoris Protein Expr. Purif. 8 1996 476 482
    • (1996) Protein Expr. Purif. , vol.8 , pp. 476-482
    • Rosenfeld, S.A.1    Nadeau, D.2    Tirado, J.3    Hollis, G.F.4    Knabb, R.M.5    Jia, S.6
  • 31
    • 0033815534 scopus 로고    scopus 로고
    • Production and characterization of recombinant guamerin, an elastase-specific inhibitor, in the methylotrophic yeast Pichia pastoris
    • K.Y. Kim, H.K. Lim, K.J. Lee, D.H. Park, K.W. Kang, S.I. Chung, and K.H. Jung Production and characterization of recombinant guamerin, an elastase-specific inhibitor, in the methylotrophic yeast Pichia pastoris Protein Expr. Purif. 20 2000 1 9
    • (2000) Protein Expr. Purif. , vol.20 , pp. 1-9
    • Kim, K.Y.1    Lim, H.K.2    Lee, K.J.3    Park, D.H.4    Kang, K.W.5    Chung, S.I.6    Jung, K.H.7
  • 33
    • 0029443619 scopus 로고
    • Expression of a synthetic gene encoding the anticoagulant-antimetastatic protein ghilanten by the methylotropic yeast Pichia pastoris
    • R.G. Brankamp, K. Sreekrishna, P.L. Smith, D.T. Blankenship, and A.D. Cardin Expression of a synthetic gene encoding the anticoagulant-antimetastatic protein ghilanten by the methylotropic yeast Pichia pastoris Protein Expr. Purif. 6 1995 813 820
    • (1995) Protein Expr. Purif. , vol.6 , pp. 813-820
    • Brankamp, R.G.1    Sreekrishna, K.2    Smith, P.L.3    Blankenship, D.T.4    Cardin, A.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.