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Volumn 126, Issue 5, 1999, Pages 905-911

Refolding and recovery of recombinant human matrix metalloproteinase 7 (matrilysin) from inclusion bodies expressed by Escherichia coli

Author keywords

Inclusion bodies; Matrilysin; Matrix metalloproteinase; Proteolysis; Refolding

Indexed keywords

MATRILYSIN;

EID: 0032731203     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022533     Document Type: Article
Times cited : (64)

References (40)
  • 1
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner, J.F., Jr. (1991) Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5, 2145-2155
    • (1991) FASEB J. , vol.5 , pp. 2145-2155
    • Woessner J.F., Jr.1
  • 2
    • 0026896029 scopus 로고
    • The matrix-degrading metalloproteinases
    • Matrisian, L.M. (1992) The matrix-degrading metalloproteinases. BioEssays 14, 455-463
    • (1992) BioEssays , vol.14 , pp. 455-463
    • Matrisian, L.M.1
  • 3
    • 0024318368 scopus 로고
    • Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members
    • Quantin, B., Murphy, G., and Breathnach, R. (1989) Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members. Biochemistry 28, 5327-5334
    • (1989) Biochemistry , vol.28 , pp. 5327-5334
    • Quantin, B.1    Murphy, G.2    Breathnach, R.3
  • 4
    • 0023716802 scopus 로고
    • Purification and properties of a small latent matrix metallo-proteinase of the rat uterus
    • Woessner, J.F., Jr. and Taplin, C.J. (1988) Purification and properties of a small latent matrix metallo-proteinase of the rat uterus. J. Biol. Chem. 263, 16918-16925
    • (1988) J. Biol. Chem. , vol.263 , pp. 16918-16925
    • Woessner J.F., Jr.1    Taplin, C.J.2
  • 5
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart, H.E. and Birkedal-Hansen, H. (1990) The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. USA 87, 5578-5582
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 6
    • 0029030448 scopus 로고
    • Matrilysin-inhibitor complexes: Common themes among metalloproteases
    • Browner, M.F., Smith, W.W., and Castelhano, A.L. (1995) Matrilysin-inhibitor complexes: common themes among metalloproteases. Biochemistry 34, 6602-6610
    • (1995) Biochemistry , vol.34 , pp. 6602-6610
    • Browner, M.F.1    Smith, W.W.2    Castelhano, A.L.3
  • 7
    • 0025647386 scopus 로고
    • Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line
    • Miyazaki, K., Hattori, Y., Umenishi, F., Yasumitsu, H., and Umeda, M. (1990) Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line. Cancer Res. 50, 7758-7764
    • (1990) Cancer Res. , vol.50 , pp. 7758-7764
    • Miyazaki, K.1    Hattori, Y.2    Umenishi, F.3    Yasumitsu, H.4    Umeda, M.5
  • 10
    • 0029151472 scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases in human gliomas
    • Nakano, A., Tani, E., Miyazaki, K., Yamamoto, Y., and Furuyama, J. (1995) Matrix metalloproteinases and tissue inhibitors of metalloproteinases in human gliomas. J. Neurosurg. 83, 298-307
    • (1995) J. Neurosurg. , vol.83 , pp. 298-307
    • Nakano, A.1    Tani, E.2    Miyazaki, K.3    Yamamoto, Y.4    Furuyama, J.5
  • 12
    • 0025895193 scopus 로고
    • Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan
    • Murphy, G., Cockett, M.I., Ward, R.V., and Docherty, A.J.P. (1991) Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. Biochem. J. 277, 277-279
    • (1991) Biochem. J. , vol.277 , pp. 277-279
    • Murphy, G.1    Cockett, M.I.2    Ward, R.V.3    Docherty, A.J.P.4
  • 14
    • 0026674106 scopus 로고
    • Gene synthesis and expression in E. coli for pump, a human matrix metalloproteinase
    • Ye, Q.Z., Johnson, L.L., and Baragi, V. (1992) Gene synthesis and expression in E. coli for pump, a human matrix metalloproteinase. Biochem. Biophys. Res. Commun. 186, 143-149
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 143-149
    • Ye, Q.Z.1    Johnson, L.L.2    Baragi, V.3
  • 16
    • 0029785284 scopus 로고    scopus 로고
    • Production of recombinant human matrix metalloproteinase 7 (matrilysin) with potential role in tumor invasion by refolding from Escherichia coli inclusion bodies and development of sandwich ELISA of MMP-7
    • Kihira, Y., Mon, K., Miyazaki, K., and Matsuo, Y. (1996) Production of recombinant human matrix metalloproteinase 7 (matrilysin) with potential role in tumor invasion by refolding from Escherichia coli inclusion bodies and development of sandwich ELISA of MMP-7. Urol. Oncol. 2, 20-26
    • (1996) Urol. Oncol. , vol.2 , pp. 20-26
    • Kihira, Y.1    Mon, K.2    Miyazaki, K.3    Matsuo, Y.4
  • 17
    • 0029875424 scopus 로고    scopus 로고
    • Purification and refolding of recombinant human proMMP-7 (pro-matrilysin) expressed in Escherichia coli and its characterization
    • Itoh, M., Masuda, K., Ito, Y., Akizawa, T., Yoshioka, M., Imai, K., Okada, Y., and Seiki, M. (1996) Purification and refolding of recombinant human proMMP-7 (pro-matrilysin) expressed in Escherichia coli and its characterization. J. Biochem. 119, 667-673
    • (1996) J. Biochem. , vol.119 , pp. 667-673
    • Itoh, M.1    Masuda, K.2    Ito, Y.3    Akizawa, T.4    Yoshioka, M.5    Imai, K.6    Okada, Y.7    Seiki, M.8
  • 18
    • 0028834866 scopus 로고
    • Purification of human matrilysin produced in Escherichia coli and characterization using a new optimized fluorogenic peptide substrate
    • Welch, A.R., Holman,C.M., Browner, M.F., Gehring, M.R., Kan, C.-C., and Van Wart, H.E. (1995) Purification of human matrilysin produced in Escherichia coli and characterization using a new optimized fluorogenic peptide substrate. Arch. Biochem. Biophys. 324, 59-64
    • (1995) Arch. Biochem. Biophys. , vol.324 , pp. 59-64
    • Welch, A.R.1    Holman, C.M.2    Browner, M.F.3    Gehring, M.R.4    Kan, C.-C.5    Van Wart, H.E.6
  • 19
    • 0029768642 scopus 로고    scopus 로고
    • Metal and pH dependence of heptapeptide catalysis by human matrilysin
    • Cha, J., Pedersen, M., and Auld, D.S. (1996) Metal and pH dependence of heptapeptide catalysis by human matrilysin. Biochemistry 35, 15831-15838
    • (1996) Biochemistry , vol.35 , pp. 15831-15838
    • Cha, J.1    Pedersen, M.2    Auld, D.S.3
  • 21
    • 0026505650 scopus 로고
    • A novel coumarin-labelled peptide for sensitive continuous assays of matrix metalloproteinases
    • Knight, C.G., Willenbrock, F., and Murphy, G. (1992) A novel coumarin-labelled peptide for sensitive continuous assays of matrix metalloproteinases. FEBS Lett. 296, 263-266
    • (1992) FEBS Lett. , vol.296 , pp. 263-266
    • Knight, C.G.1    Willenbrock, F.2    Murphy, G.3
  • 22
    • 0029863639 scopus 로고    scopus 로고
    • Effect of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts
    • Inouye, K., Lee, S.-B., and Tonomura, B. (1996) Effect of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts. Biochem. J. 315, 133-138
    • (1996) Biochem. J. , vol.315 , pp. 133-138
    • Inouye, K.1    Lee, S.-B.2    Tonomura, B.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0026775558 scopus 로고
    • Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloproteinases
    • Crabbe, T., Willenbrock, F., Eaton, D., Hynds, P., Carne, A.F., Murphy, G., and Docherty, A.J.P. (1992) Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloproteinases. Biochemistry 31, 8500-8507
    • (1992) Biochemistry , vol.31 , pp. 8500-8507
    • Crabbe, T.1    Willenbrock, F.2    Eaton, D.3    Hynds, P.4    Carne, A.F.5    Murphy, G.6    Docherty, A.J.P.7
  • 25
    • 0022531818 scopus 로고
    • Purification and characterization of recombinant single-chain urokinase produced in Escherichia coli
    • Winkler, M.E. and Blaber, M. (1986) Purification and characterization of recombinant single-chain urokinase produced in Escherichia coli. Biochemistry 25, 4041-4045
    • (1986) Biochemistry , vol.25 , pp. 4041-4045
    • Winkler, M.E.1    Blaber, M.2
  • 26
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner, J. and Rudolph, R. (1991) Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Bio/Technology 9, 157-162
    • (1991) Bio/Technology , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 27
    • 0026792807 scopus 로고
    • A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies
    • Buchner, J., Pstan, I., and Brinkmann, U. (1992) A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal. Biochem. 295, 263-270
    • (1992) Anal. Biochem. , vol.295 , pp. 263-270
    • Buchner, J.1    Pstan, I.2    Brinkmann, U.3
  • 28
    • 0030579519 scopus 로고    scopus 로고
    • Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies
    • Arora, D. and Khanna, N. (1996) Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies. J. Biotechnol. 52, 127-133
    • (1996) J. Biotechnol. , vol.52 , pp. 127-133
    • Arora, D.1    Khanna, N.2
  • 29
    • 0031688064 scopus 로고    scopus 로고
    • Renaturation of recombinant human neurotrophin-3 from inclusion bodies using a suppressor agent of aggregation
    • Suenaga, M., Ohmae, H., Tsuji, S., Itoh, T., and Nishimura, O. (1998) Renaturation of recombinant human neurotrophin-3 from inclusion bodies using a suppressor agent of aggregation. Biotechnol. Appl. Biochem. 28, 119-124
    • (1998) Biotechnol. Appl. Biochem. , vol.28 , pp. 119-124
    • Suenaga, M.1    Ohmae, H.2    Tsuji, S.3    Itoh, T.4    Nishimura, O.5
  • 30
    • 0033102489 scopus 로고    scopus 로고
    • Refolding, purification, and characterization of a loop deletion mutant of human Bcl-2 from bacterial inclusion bodies
    • Anderson, M., Blowers, D., Hewitt, N., Hedge, P., Breeze, A., Hampton, I., and Taylor, I. (1999) Refolding, purification, and characterization of a loop deletion mutant of human Bcl-2 from bacterial inclusion bodies. Protein Exp. Purif. 15, 162-170
    • (1999) Protein Exp. Purif. , vol.15 , pp. 162-170
    • Anderson, M.1    Blowers, D.2    Hewitt, N.3    Hedge, P.4    Breeze, A.5    Hampton, I.6    Taylor, I.7
  • 32
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee, B.L. and Auld, D.S. (1990) Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29, 5647-5659
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 33
    • 0026799337 scopus 로고
    • Effects of salts on thermolysin: Activation of hydrolysis and synthesis of N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, and a unique change in the absorption spectrum of thermolysin
    • Inouye, K. (1992) Effects of salts on thermolysin: Activation of hydrolysis and synthesis of N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, and a unique change in the absorption spectrum of thermolysin. J. Biochem. 112, 335-340
    • (1992) J. Biochem. , vol.112 , pp. 335-340
    • Inouye, K.1
  • 34
    • 0028129002 scopus 로고
    • A spectrophotometric study on the interaction of thermolysin with chloride and bromide ions, and the state of tryptophyl residue 115
    • Inouye, K., Kuzuya, K., and Tonomura, B. (1994) A spectrophotometric study on the interaction of thermolysin with chloride and bromide ions, and the state of tryptophyl residue 115. J. Biochem. 116, 530-535
    • (1994) J. Biochem. , vol.116 , pp. 530-535
    • Inouye, K.1    Kuzuya, K.2    Tonomura, B.3
  • 35
    • 0030772527 scopus 로고    scopus 로고
    • Effects of pH, temperature, and alcohols on the remarkable activation of thermolysin by salts
    • Inouye, K., Lee, S.-B., Nambu, K., and Tonomura, B. (1997) Effects of pH, temperature, and alcohols on the remarkable activation of thermolysin by salts. J. Biochem. 122, 358-364
    • (1997) J. Biochem. , vol.122 , pp. 358-364
    • Inouye, K.1    Lee, S.-B.2    Nambu, K.3    Tonomura, B.4
  • 36
    • 0031979332 scopus 로고    scopus 로고
    • Effect of salts on the solubility od thermolysin: A remarkable increase in the solubility as well as the activity by the addition of salts without aggregation or dispersion of thermolysin
    • Inouye, K., Kuzuya, K., and Tonomura, B. (1998) Effect of salts on the solubility od thermolysin: A remarkable increase in the solubility as well as the activity by the addition of salts without aggregation or dispersion of thermolysin. J. Biochem. 123, 847-852
    • (1998) J. Biochem. , vol.123 , pp. 847-852
    • Inouye, K.1    Kuzuya, K.2    Tonomura, B.3
  • 37
    • 0032517347 scopus 로고    scopus 로고
    • Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity
    • Inouye, K., Kuzuya, K., and Tonomura, B. (1998) Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity. Biochim. Biophys. Acta 1388, 209-214
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 209-214
    • Inouye, K.1    Kuzuya, K.2    Tonomura, B.3
  • 38
    • 0032038895 scopus 로고    scopus 로고
    • Need for aromatic residue at position 115 for proteolytic activity found by site-directed mutagenesis of tryptophan 115 in thermolysin
    • Inouye, K., Mazda, N., and Kubo, M. (1998) Need for aromatic residue at position 115 for proteolytic activity found by site-directed mutagenesis of tryptophan 115 in thermolysin. Biosci. Biotechnol. Biochem. 62, 798-800
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 798-800
    • Inouye, K.1    Mazda, N.2    Kubo, M.3
  • 39
    • 0033067897 scopus 로고    scopus 로고
    • Mechanism of thermostability in thermolysin. Analysis of subsite S2 mutant enzymes of thermolysin
    • Kubo, M., Itoh, K., Nishikawa, K., Hasumi, F., and Inouye, K. (1999) Mechanism of thermostability in thermolysin. Analysis of subsite S2 mutant enzymes of thermolysin. Lett. Appl. Microbiol. 28, 431-434
    • (1999) Lett. Appl. Microbiol. , vol.28 , pp. 431-434
    • Kubo, M.1    Itoh, K.2    Nishikawa, K.3    Hasumi, F.4    Inouye, K.5
  • 40
    • 0031848311 scopus 로고    scopus 로고
    • Effects of nitration and amination of tyrosyl residues in thermolysin on its hydrolytic activity and its remarkable activation by salts
    • Inouye, K., Lee, S.-B., and Tonomura, B. (1998) Effects of nitration and amination of tyrosyl residues in thermolysin on its hydrolytic activity and its remarkable activation by salts. J. Biochem. 124, 72-78
    • (1998) J. Biochem. , vol.124 , pp. 72-78
    • Inouye, K.1    Lee, S.-B.2    Tonomura, B.3


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