메뉴 건너뛰기




Volumn 7, Issue 2, 2009, Pages 275-281

Refolding of β-galactosidase: Microfluidic device for reagent metering and mixing and quantification of refolding yield

Author keywords

Galactosidase; Combinatorial; Microfluidic; Protein refolding

Indexed keywords

AUTOMATED CONTROL; COMBINATORIAL; CONVENTIONAL TECHNIQUES; DRUG DISCOVERY; FLUORESCENT MOLECULES; GALACTOPYRANOSIDE; GALACTOSIDASES; GLASS DEVICES; MICRO-FLUIDIC DEVICES; MICROFLUIDIC VALVES; MULTI-LAYERED; OFF-CHIP; ON CHIPS; OPTICAL DETECTION; PROTEIN PHARMACEUTICALS; PROTEIN REFOLDING; REFOLDING; ROBOTIC SYSTEMS; SAMPLE VOLUME;

EID: 68349096074     PISSN: 16134982     EISSN: 16134990     Source Type: Journal    
DOI: 10.1007/s10404-008-0388-z     Document Type: Article
Times cited : (8)

References (34)
  • 1
    • 0029881740 scopus 로고    scopus 로고
    • Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli b-galactosidase
    • Ayling A, Beneyx F (1996) Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli b-galactosidase. Protein Sci 5(3):478-487
    • (1996) Protein Sci , vol.5 , Issue.3 , pp. 478-487
    • Ayling, A.1    Beneyx, F.2
  • 2
    • 0014193191 scopus 로고
    • Regulation of the lac operon. Recent studies on the regulation of lactose metabolism in Escherichia coli support the operon model
    • Beckwith JR (1967) Regulation of the lac operon. Recent studies on the regulation of lactose metabolism in Escherichia coli support the operon model. Science 156(3775):597-604
    • (1967) Science , vol.156 , Issue.3775 , pp. 597-604
    • Beckwith, J.R.1
  • 3
    • 0035183611 scopus 로고    scopus 로고
    • A microfabricated rotary pump
    • Chou H-P, Unger MA et al (2001) A microfabricated rotary pump. Biomed Microdevices 3(4):323-330
    • (2001) Biomed Microdevices , vol.3 , Issue.4 , pp. 323-330
    • Chou, H.-P.1    Unger, M.A.2
  • 4
    • 0001165802 scopus 로고
    • Purification, composition, and molecular weight of the b-galactosidase of Escherichia coli K12
    • Craven GR, Steers E Jr et al (1965) Purification, composition, and molecular weight of the b-galactosidase of Escherichia coli K12. J Biol Chem 240(6):2468-2477
    • (1965) J Biol Chem , vol.240 , Issue.6 , pp. 2468-2477
    • Craven, G.R.1    Steers Jr., E.2
  • 5
    • 0032403465 scopus 로고    scopus 로고
    • Rapid prototyping of microfluidic systems in poly(dimethylsiloxane)
    • Duffy DC, McDonald JC et al (1998) Rapid prototyping of microfluidic systems in poly(dimethylsiloxane). Anal Chem 70(23):4974-4984
    • (1998) Anal Chem , vol.70 , Issue.23 , pp. 4974-4984
    • Duffy, D.C.1    McDonald, J.C.2
  • 6
    • 0017875606 scopus 로고
    • Amino acid sequence of b-galactosidase. XI. Peptide ordering procedures and the complete sequence
    • Fowler AV, Zabin I (1978) Amino acid sequence of b-galactosidase. XI. Peptide ordering procedures and the complete sequence. J Biol Chem 253(15):5521-5525
    • (1978) J Biol Chem , vol.253 , Issue.15 , pp. 5521-5525
    • Fowler, A.V.1    Zabin, I.2
  • 7
    • 39049163759 scopus 로고    scopus 로고
    • Microfluidic devices for terahertz spectroscopy of biomolecules
    • George PA, Hui W et al (2008) Microfluidic devices for terahertz spectroscopy of biomolecules. Opt Express 16(3):1577-1582
    • (2008) Opt Express , vol.16 , Issue.3 , pp. 1577-1582
    • George, P.A.1    Hui, W.2
  • 8
    • 1842410676 scopus 로고    scopus 로고
    • Oxidative renaturation of lysozyme at high concentrations
    • Hevehan DL, De Bernardez Clark E (1997) Oxidative renaturation of lysozyme at high concentrations. Biotechnol Bioeng 54(3):221-230
    • (1997) Biotechnol Bioeng , vol.54 , Issue.3 , pp. 221-230
    • Hevehan, D.L.1    De Bernardez Clark, E.2
  • 9
    • 0026044752 scopus 로고
    • Kinetic fluorescence measurement of fluorescein di-beta- d -galactoside hydrolysis by beta-galactosidase: Intermediate channeling in stepwise catalysis by a free single enzyme
    • Huang ZJ (1991) Kinetic fluorescence measurement of fluorescein di-beta- d -galactoside hydrolysis by beta-galactosidase: Intermediate channeling in stepwise catalysis by a free single enzyme. Biochemistry 30(35):8535-8540
    • (1991) Biochemistry , vol.30 , Issue.35 , pp. 8535-8540
    • Huang, Z.J.1
  • 10
    • 0021506865 scopus 로고
    • Binding and reactivity at the glucose site of galactosyl-b-galactosidase (Escherichia coli)
    • Huber RE, Gaunt MT et al (1984) Binding and reactivity at the glucose site of galactosyl-b-galactosidase (Escherichia coli). Arch Biochem Biophys 234(1):151-160
    • (1984) Arch Biochem Biophys , vol.234 , Issue.1 , pp. 151-160
    • Huber, R.E.1    Gaunt, M.T.2
  • 11
    • 0017170906 scopus 로고
    • A quantitation of the factors which affect the hydrolase and transgalactosylase activities of b-galactosidase (E. coli) on lactose
    • Huber RE, Kurz G et al (1976) A quantitation of the factors which affect the hydrolase and transgalactosylase activities of b-galactosidase (E. coli) on lactose. Biochemistry 15(9):1994-2001
    • (1976) Biochemistry , vol.15 , Issue.9 , pp. 1994-2001
    • Huber, R.E.1    Kurz, G.2
  • 12
    • 54249116230 scopus 로고
    • Genetic regulatory mechanisms in the synthesis of proteins
    • Jacob F, Monod J (1961) Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol 3:318-356
    • (1961) J Mol Biol , vol.3 , pp. 318-356
    • Jacob, F.1    Monod, J.2
  • 13
    • 0028178377 scopus 로고
    • Three-dimensional structure of b-galactosidase from E. coli
    • Jacobson RH, Zhang XJ et al (1994) Three-dimensional structure of b-galactosidase from E. coli. Nature 369(6483):761-766
    • (1994) Nature , vol.369 , Issue.6483 , pp. 761-766
    • Jacobson, R.H.1    Zhang, X.J.2
  • 14
    • 0020689671 scopus 로고
    • Sequence of the lacZ gene of Escherichia coli
    • Kalnins A, Otto K et al (1983) Sequence of the lacZ gene of Escherichia coli. EMBO J 2(4):593-597
    • (1983) EMBO J , vol.2 , Issue.4 , pp. 593-597
    • Kalnins, A.1    Otto, K.2
  • 15
    • 0007879761 scopus 로고
    • High-resolution electron microscopy on highly purified b-galactosidase from Escherichia coli
    • Karlsson U, Koorajian S et al (1964) High-resolution electron microscopy on highly purified b-galactosidase from Escherichia coli. J Ultra Mol Struct R 10(5-6):457-469
    • (1964) J Ultra Mol Struct R , vol.10 , Issue.5-6 , pp. 457-469
    • Karlsson, U.1    Koorajian, S.2
  • 16
    • 33749990843 scopus 로고    scopus 로고
    • Kinetic measurements of protein conformation in a microchip
    • Kerby MB, Lee J et al (2006) Kinetic measurements of protein conformation in a microchip. Biotechnol Progr 22(5):1416-1425
    • (2006) Biotechnol Progr , vol.22 , Issue.5 , pp. 1416-1425
    • Kerby, M.B.1    Lee, J.2
  • 17
    • 2342455750 scopus 로고    scopus 로고
    • Microfluidic valve with cored glass microneedle for microinjection
    • Lee S, Jeong W et al (2003) Microfluidic valve with cored glass microneedle for microinjection. Lab Chip 3(3):164-167
    • (2003) Lab Chip , vol.3 , Issue.3 , pp. 164-167
    • Lee, S.1    Jeong, W.2
  • 18
    • 0014511136 scopus 로고
    • Purification and characterization of the multiple forms of b-galactosidase of Escherichia coli
    • Marchesi SL, Steers E Jr et al (1969) Purification and characterization of the multiple forms of b-galactosidase of Escherichia coli. BBA Protein Struct M 181(1):20-34
    • (1969) BBA Protein Struct M , vol.181 , Issue.1 , pp. 20-34
    • Marchesi, S.L.1    Steers Jr., E.2
  • 19
    • 0032500678 scopus 로고    scopus 로고
    • Folding and association of b-galactosidase
    • Nichtl A, Buchner J et al (1998) Folding and association of b-galactosidase. J Mol Biol 282(5):1083-1091
    • (1998) J Mol Biol , vol.282 , Issue.5 , pp. 1083-1091
    • Nichtl, A.1    Buchner, J.2
  • 20
    • 0023989715 scopus 로고
    • Fluorescence-activated cell analysis and sorting of viable mammalian cells based on b- d -galactosidase activity after transduction of Escherichia coli lacZ
    • Nolan GP, Fiering S et al (1988) Fluorescence-activated cell analysis and sorting of viable mammalian cells based on b- d -galactosidase activity after transduction of Escherichia coli lacZ. Proc Natl Acad Sci USA 85(8):2603-2607
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.8 , pp. 2603-2607
    • Nolan, G.P.1    Fiering, S.2
  • 21
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • Pelton JT, McLean LR (2000) Spectroscopic methods for analysis of protein secondary structure. Anal Biochem 277(2):167-176
    • (2000) Anal Biochem , vol.277 , Issue.2 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 22
    • 0035926229 scopus 로고    scopus 로고
    • Time resolved collapse of a folding protein observed with small angle X-ray scattering
    • Pollack L, Tate MW et al (2001) Time resolved collapse of a folding protein observed with small angle X-ray scattering. Phys Rev Lett 86(21):4962-4965
    • (2001) Phys Rev Lett , vol.86 , Issue.21 , pp. 4962-4965
    • Pollack, L.1    Tate, M.W.2
  • 23
    • 73649195476 scopus 로고
    • Fluorogenic substrates for b- d -galactosidases and phosphatases derived from fluorescein (3, 6-dihydroxyfiuoran) and its mono-methyl ether
    • Rotman B, Zderic JA et al (1963) Fluorogenic substrates for b- d -galactosidases and phosphatases derived from fluorescein (3, 6-dihydroxyfiuoran) and its mono-methyl ether. Proc Natl Acad Sci USA 50(1):1-6
    • (1963) Proc Natl Acad Sci USA , vol.50 , Issue.1 , pp. 1-6
    • Rotman, B.1    Zderic, J.A.2
  • 24
    • 0014200003 scopus 로고
    • Effect of urea on subunit interaction of b-galactosidase from Escherichia coli K12
    • Shifrin S, Steers E Jr (1967) Effect of urea on subunit interaction of b-galactosidase from Escherichia coli K12. BBA Protein Struct M 133(3):463-471
    • (1967) BBA Protein Struct M , vol.133 , Issue.3 , pp. 463-471
    • Shifrin, S.1    Steers Jr., E.2
  • 25
    • 33645982880 scopus 로고    scopus 로고
    • Refolding studies using pressure: The folding landscape of lysozyme in the pressure-temperature plane
    • Smeller L, Meersman F et al (2006) Refolding studies using pressure: The folding landscape of lysozyme in the pressure-temperature plane. BBA Proteins Proteom 1764(3):497-505
    • (2006) BBA Proteins Proteom , vol.1764 , Issue.3 , pp. 497-505
    • Smeller, L.1    Meersman, F.2
  • 26
    • 0017303552 scopus 로고
    • Antibody as an immunological probe for studying the refolding of bovine serum albumin. I. The catalysis of reoxidation of reduced bovine serum albumin by glutathione and a disulfide interchange enzyme
    • Teale JM, Benjamin DC (1976a) Antibody as an immunological probe for studying the refolding of bovine serum albumin. I. The catalysis of reoxidation of reduced bovine serum albumin by glutathione and a disulfide interchange enzyme. J Biol Chem 251(15):4603-4608
    • (1976) J Biol Chem , vol.251 , Issue.15 , pp. 4603-4608
    • Teale, J.M.1    Benjamin, D.C.2
  • 27
    • 0017303535 scopus 로고
    • Antibody as an immunological probe for studying the refolding of bovine serum albumin. II. Evidence for the independent refolding of the domains of the molecule
    • Teale JM, Benjamin DC (1976b) Antibody as an immunological probe for studying the refolding of bovine serum albumin. II. Evidence for the independent refolding of the domains of the molecule. J Biol Chem 251(15):4609-4615
    • (1976) J Biol Chem , vol.251 , Issue.15 , pp. 4609-4615
    • Teale, J.M.1    Benjamin, D.C.2
  • 28
    • 0037131390 scopus 로고    scopus 로고
    • Microfluidic large-scale integration
    • Thorsen T, Maerkl SJ et al (2002) Microfluidic large-scale integration. Science 298(5593):580-584
    • (2002) Science , vol.298 , Issue.5593 , pp. 580-584
    • Thorsen, T.1    Maerkl, S.J.2
  • 29
    • 0014669735 scopus 로고
    • Effect of divalent cations and protein concentration upon renaturation of b-galactosidase from E. coli
    • Ullmann A, Monod J (1969) Effect of divalent cations and protein concentration upon renaturation of b-galactosidase from E. coli. Biochem Biophys Res Commun 35(1):35-42
    • (1969) Biochem Biophys Res Commun , vol.35 , Issue.1 , pp. 35-42
    • Ullmann, A.1    Monod, J.2
  • 30
    • 0034615958 scopus 로고    scopus 로고
    • Monolithic microfabricated valves and pumps by multilayer soft lithography
    • Unger MA, Chou H-P et al (2000) Monolithic microfabricated valves and pumps by multilayer soft lithography. Science 288(5463):113-116
    • (2000) Science , vol.288 , Issue.5463 , pp. 113-116
    • Unger, M.A.1    Chou, H.-P.2
  • 32
    • 3542998691 scopus 로고    scopus 로고
    • Two-dimensional protein separation with advanced sample and buffer isolation using microfluidic valves
    • Wang Y-C, Choi MH et al (2004) Two-dimensional protein separation with advanced sample and buffer isolation using microfluidic valves. Anal Chem 76(15):4426-4431
    • (2004) Anal Chem , vol.76 , Issue.15 , pp. 4426-4431
    • Wang, Y.-C.1    Choi, M.H.2
  • 33
    • 0020036666 scopus 로고
    • Cytoplasmic inclusion bodies in Escherichia coli producing biosynthetic human insulin proteins
    • Williams DC, Van Frank RM et al (1982) Cytoplasmic inclusion bodies in Escherichia coli producing biosynthetic human insulin proteins. Science 215(4533):687-689
    • (1982) Science , vol.215 , Issue.4533 , pp. 687-689
    • Williams, D.C.1    Van Frank, R.M.2
  • 34
    • 0018788361 scopus 로고
    • Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation
    • Zettlmeissl G, Rudolph R et al (1979) Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry 18(25):5567-5571
    • (1979) Biochemistry , vol.18 , Issue.25 , pp. 5567-5571
    • Zettlmeissl, G.1    Rudolph, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.