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Volumn 13, Issue 9, 1999, Pages 637-641

Lysozyme reactivation using immobilized molecular chaperonin GroEL

Author keywords

GroEL; Immobilization; Lysozyme; Reactivation; Refolding

Indexed keywords

CHAPERONIN; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME REACTIVATION; IMMOBILIZED PROTEIN; LYSOZYME; PH; PROTEIN FOLDING;

EID: 0032873832     PISSN: 0951208X     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1008920515993     Document Type: Article
Times cited : (6)

References (10)
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    • Fisher MT (1992) Promotion of the in vitro renaturation of dodecametric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP. Biochemistry 31: 3955-3963.
    • (1992) Biochemistry , vol.31 , pp. 3955-3963
    • Fisher, M.T.1
  • 3
    • 0032031152 scopus 로고    scopus 로고
    • Recovery and reuse of the molecular chaperone GroEL for in vitro protein refolding
    • Guise AD, Chaudhuri JB (1998) Recovery and reuse of the molecular chaperone GroEL for in vitro protein refolding. Biotechnol. Prog. 14: 343-346.
    • (1998) Biotechnol. Prog. , vol.14 , pp. 343-346
    • Guise, A.D.1    Chaudhuri, J.B.2
  • 4
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F-U (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.-U.1
  • 5
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto T, Yagishita K (1971) A simple activity measurement of lysozyme. Agric. Biol. Chem. 35: 1154-1156.
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 7
    • 0022569969 scopus 로고
    • DNA fragment containing the groE genes can suppress mutations in Escherichia coli dnaA genes
    • Jenkins AJ, March JB, Oliver IR, Masters M (1986) DNA fragment containing the groE genes can suppress mutations in Escherichia coli dnaA genes. Mol. Gen. Genet. 202: 446-454.
    • (1986) Mol. Gen. Genet. , vol.202 , pp. 446-454
    • Jenkins, A.J.1    March, J.B.2    Oliver, I.R.3    Masters, M.4
  • 8
    • 0025820393 scopus 로고
    • Chaperonins facilitate the in vitro folding of monometric mitochondrial rhodanase
    • Mendoza JA, Rogers E, Lorimer GH, Horowitz PM (1991) Chaperonins facilitate the in vitro folding of monometric mitochondrial rhodanase. J. Biol. Chem. 266: 13044-13049.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13044-13049
    • Mendoza, J.A.1    Rogers, E.2    Lorimer, G.H.3    Horowitz, P.M.4
  • 9
    • 0029637144 scopus 로고
    • Protein refolding and inactivation during bioseparation: Bopprocessing implications
    • Sadana A (1995) Protein refolding and inactivation during bioseparation: Bopprocessing implications. Biotechnol. Bioeng. 48: 481-489.
    • (1995) Biotechnol. Bioeng. , vol.48 , pp. 481-489
    • Sadana, A.1
  • 10
    • 0030796979 scopus 로고    scopus 로고
    • Reactivation of thermally inactivated enzymes by free and immobilized chaperonin GroEL/ES
    • Teshima T, Kondo A, Fukuda H (1997) Reactivation of thermally inactivated enzymes by free and immobilized chaperonin GroEL/ES. Appl. Microbiol. Biotechnol. 48: 41-46.
    • (1997) Appl. Microbiol. Biotechnol. , vol.48 , pp. 41-46
    • Teshima, T.1    Kondo, A.2    Fukuda, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.