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Volumn 31, Issue 4, 1996, Pages 341-345

Effective refolding of fully reduced lysozyme with a flow-type reactor

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EID: 0030019343     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/0032-9592(95)00069-0     Document Type: Article
Times cited : (23)

References (12)
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    • Mitraki, A.1    King, J.2
  • 2
    • 0027908939 scopus 로고
    • Isolation, renaturation and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies
    • Fischer, B., Sumner, I. & Goodenough, P., Isolation, renaturation and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies. Biotechnol. Bioeng., 41 (1993) 3-13.
    • (1993) Biotechnol. Bioeng. , vol.41 , pp. 3-13
    • Fischer, B.1    Sumner, I.2    Goodenough, P.3
  • 4
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    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner, J. & Rudolph, R., Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Bio/Technol., 9 (1991) 157-62.
    • (1991) Bio/Technol. , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 5
    • 0023334384 scopus 로고
    • , Direct expression of a synthetic somatomedine C gene in Escherichia coli by use of two-cistron system
    • Saito, Y., Ishii, Y., Niwa, M. & Ueda, I., Direct expression of a synthetic somatomedine C gene in Escherichia coli by use of two-cistron system. J. Biochem., 101 (1987) 1281-8.
    • (1987) J. Biochem. , vol.101 , pp. 1281-1288
    • Saito, Y.1    Ishii, Y.2    Niwa, M.3    Ueda, I.4
  • 7
    • 0026640258 scopus 로고
    • Effects of the chaperonin Gro E on the refolding of typtophanase from Escherichia coli
    • Mizobata, T., Akiyama, Y., Ito, K., Yumoto, N. & Kawata, Y., Effects of the chaperonin Gro E on the refolding of typtophanase from Escherichia coli. J. Biol. Chem., 267 (1992) 17773-9.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17773-17779
    • Mizobata, T.1    Akiyama, Y.2    Ito, K.3    Yumoto, N.4    Kawata, Y.5
  • 9
    • 0016744271 scopus 로고
    • Refolding of reduced, denatured trypsinogen and trypsin immobilized on agarose beads
    • Sinha, N. K. & Light, A., Refolding of reduced, denatured trypsinogen and trypsin immobilized on agarose beads. J. Biol. Chem., 250 (1975) 8624-9.
    • (1975) J. Biol. Chem. , vol.250 , pp. 8624-8629
    • Sinha, N.K.1    Light, A.2
  • 10
    • 14744269612 scopus 로고
    • Cosolvent assisted protein refolding
    • Cleland, J. L. & Wang, D. I. C., Cosolvent assisted protein refolding. Bio/Technol., 8 (1990) 1274-8.
    • (1990) Bio/Technol. , vol.8 , pp. 1274-1278
    • Cleland, J.L.1    Wang, D.I.C.2
  • 11
    • 0027169506 scopus 로고
    • 'Loose folding' and 'delayed oxidation' procedures successfully applied for refolding of fully reduced hen egg white lysozyme
    • Matsubara, M., Nohara, D., Kurimoto, E., Kuroda, Y. & Sakai, T., 'Loose folding' and 'delayed oxidation' procedures successfully applied for refolding of fully reduced hen egg white lysozyme. Chem. Pharm. Bull., 41 (1993) 1207-10.
    • (1993) Chem. Pharm. Bull. , vol.41 , pp. 1207-1210
    • Matsubara, M.1    Nohara, D.2    Kurimoto, E.3    Kuroda, Y.4    Sakai, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.