메뉴 건너뛰기




Volumn 168, Issue 4, 2013, Pages 506-510

Employment of colorimetric enzyme assay for monitoring expression and solubility of GST fusion proteins targeted to inclusion bodies

Author keywords

GST; GST tagged proteins; Inclusion bodies; Urea

Indexed keywords

1-CHLORO-2 , 4-DINITROBENZENE; BIOACTIVE PROTEINS; DENATURING CONDITIONS; GST; INCLUSION BODIES; PROTEIN EXPRESSIONS; QUANTITATIVE MEASUREMENT; RECOMBINANT PROTEIN EXPRESSION;

EID: 84888826710     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2013.09.019     Document Type: Article
Times cited : (2)

References (26)
  • 3
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22:1399-1408.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 6
    • 0025856806 scopus 로고
    • Denaturated states of proteins
    • Dill K.A., Shortle D. Denaturated states of proteins. Annu. Rev. Biochem. 1991, 60:795-825.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 7
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • Frangioni J.V., Neel B.G. Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal. Biochem. 1993, 210:179-187.
    • (1993) Anal. Biochem. , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 10
    • 0016275313 scopus 로고
    • Glutathione S-transferases: the first enzymatic step in mercapturic acid formation
    • Habitg W.H., Pabst M.J., Jakoby W.B. Glutathione S-transferases: the first enzymatic step in mercapturic acid formation. J. Biol. Chem. 1974, 249:7130-7139.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habitg, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 11
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Eschericia coli
    • Hannig G., Makrides S.C. Strategies for optimizing heterologous protein expression in Eschericia coli. Trends Biotechnol. 1998, 16:54-60.
    • (1998) Trends Biotechnol. , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 12
    • 34447628052 scopus 로고    scopus 로고
    • Activity of recombinant GST in Escherichia coli grown on glucose and glycerol
    • Hansen R., Eriksen N.T. Activity of recombinant GST in Escherichia coli grown on glucose and glycerol. Process Biochem. 2007, 42:1259-1263.
    • (2007) Process Biochem. , vol.42 , pp. 1259-1263
    • Hansen, R.1    Eriksen, N.T.2
  • 14
    • 0032171073 scopus 로고    scopus 로고
    • Solubilization of recombinant ovine growth hormone with retention of native-like secondary structure and its refolding from the inclusion bodies of Escherichia coli
    • Khan R.H., AppaRao K.B.C., Eshwari A.N.S., Totey S.M., Panda A.K. Solubilization of recombinant ovine growth hormone with retention of native-like secondary structure and its refolding from the inclusion bodies of Escherichia coli. Biotechnol. Prog. 1998, 14:722-728.
    • (1998) Biotechnol. Prog. , vol.14 , pp. 722-728
    • Khan, R.H.1    AppaRao, K.B.C.2    Eshwari, A.N.S.3    Totey, S.M.4    Panda, A.K.5
  • 16
    • 0028931691 scopus 로고
    • Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonicum and its complex with the leading antischistosomal drug praziquantel
    • McTigue M.A., Williams D.R., Tainer J.A. Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonicum and its complex with the leading antischistosomal drug praziquantel. J. Mol. Biol. 1995, 246:21-27.
    • (1995) J. Mol. Biol. , vol.246 , pp. 21-27
    • McTigue, M.A.1    Williams, D.R.2    Tainer, J.A.3
  • 17
    • 82355181574 scopus 로고    scopus 로고
    • ATP synthase complex of Plasmodium falciparum: dimeric assembly in mitochondrial membranes and resistance to genetic disruption
    • Nina P.B., Morrisey J.M., Ganesan S.M., Ke H., Pershing A.M., Mather M.W., Vaidya A.B. ATP synthase complex of Plasmodium falciparum: dimeric assembly in mitochondrial membranes and resistance to genetic disruption. J. Biol. Chem. 2011, 286:41312-41322.
    • (2011) J. Biol. Chem. , vol.286 , pp. 41312-41322
    • Nina, P.B.1    Morrisey, J.M.2    Ganesan, S.M.3    Ke, H.4    Pershing, A.M.5    Mather, M.W.6    Vaidya, A.B.7
  • 18
    • 82255173613 scopus 로고    scopus 로고
    • Active protein aggregates produced in Escherichia coli
    • Peternal S., Komel R. Active protein aggregates produced in Escherichia coli. Int. J. Mol. Sci. 2011, 12:8275-8287.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 8275-8287
    • Peternal, S.1    Komel, R.2
  • 19
    • 33645018648 scopus 로고    scopus 로고
    • Crystal structure at 1.45-Å resolution of the major allergen endo-β-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome
    • Receveur-Brechot V., Czjzek M., Barre A., Roussel A., Peumans W.J., Van Damme E.J.M., Rouge P. Crystal structure at 1.45-Å resolution of the major allergen endo-β-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome. Proteins 2006, 63:235-242.
    • (2006) Proteins , vol.63 , pp. 235-242
    • Receveur-Brechot, V.1    Czjzek, M.2    Barre, A.3    Roussel, A.4    Peumans, W.J.5    Van Damme, E.J.M.6    Rouge, P.7
  • 20
    • 77953699543 scopus 로고    scopus 로고
    • Identification of a self-association domain in the Ewing's sarcoma protein: a novel function for arginine-glycine-glycine rich motifs?
    • Shaw D.J., Morse R., Todd A.G., Eggleton P., Lorson C.L., Young P.J. Identification of a self-association domain in the Ewing's sarcoma protein: a novel function for arginine-glycine-glycine rich motifs?. J. Biochem. 2010, 147:885-893.
    • (2010) J. Biochem. , vol.147 , pp. 885-893
    • Shaw, D.J.1    Morse, R.2    Todd, A.G.3    Eggleton, P.4    Lorson, C.L.5    Young, P.J.6
  • 21
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • Singh S.M., Panda A.K. Solubilization and refolding of bacterial inclusion body proteins. J. Biosci. Bioeng. 2005, 99:303-310.
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 22
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sorensen H.P., Mortensen K.K. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 2005, 115:113-128.
    • (2005) J. Biotechnol. , vol.115 , pp. 113-128
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 23
    • 0027509417 scopus 로고
    • TGMV replication protein AL1 preferentially binds to single-stranded DNA from the common region
    • Thommes P., Osman T.A.M., Hayes R.J., Buck K.W. TGMV replication protein AL1 preferentially binds to single-stranded DNA from the common region. FEBS Lett. 1993, 319:95-99.
    • (1993) FEBS Lett. , vol.319 , pp. 95-99
    • Thommes, P.1    Osman, T.A.M.2    Hayes, R.J.3    Buck, K.W.4
  • 24
    • 0344495223 scopus 로고    scopus 로고
    • Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine
    • Tsumoto K., Umetsu M., Kumagai I., Ejima D., Arakawa T. Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine. Biochem. Biophys. Res. Commun. 2003, 312:1383-1386.
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 1383-1386
    • Tsumoto, K.1    Umetsu, M.2    Kumagai, I.3    Ejima, D.4    Arakawa, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.