메뉴 건너뛰기




Volumn 15, Issue 1, 2013, Pages 57-64

Activity of the integrated on-line trypsin microreactor and nanoelectrospray emitter in acetonitrile-water co-solvent mixtures

Author keywords

Electrospray ionization; Microreactor; Nanoelectrospray; Nanofluidic integration; Trypsin

Indexed keywords

FUSED-SILICA CAPILLARIES; ION TRAP MASS SPECTROMETER; MICRO-REACTOR; NANO-ELECTROSPRAY EMITTER; NANO-ELECTROSPRAY IONIZATIONS; NANOELECTROSPRAY; NANOELECTROSPRAY IONIZATION MASS SPECTROMETRY; TRYPSIN;

EID: 84881190519     PISSN: 16134982     EISSN: 16134990     Source Type: Journal    
DOI: 10.1007/s10404-012-1134-0     Document Type: Article
Times cited : (4)

References (33)
  • 2
    • 0028046098 scopus 로고
    • Enhancement of enzyme activity in aqueous-organic solvent mixtures
    • 10.1007/BF01022403
    • Batra R, Gupta MN (1994) Enhancement of enzyme activity in aqueous-organic solvent mixtures. Biotechnol Lett 16:1059-1064
    • (1994) Biotechnol Lett , vol.16 , pp. 1059-1064
    • Batra, R.1    Gupta, M.N.2
  • 3
    • 0001665302 scopus 로고
    • Enzymes in non-Aqueous solvents
    • 10.1016/0141-0229(79)90044-9
    • Butler LG (1979) Enzymes in non-Aqueous solvents. Enzym Microb Technol 1:253-259
    • (1979) Enzym Microb Technol , vol.1 , pp. 253-259
    • Butler, L.G.1
  • 4
    • 0019585856 scopus 로고
    • Preferential hydration of bovine serum albumin in polyhydric alcohol-water mixtures
    • Gekko K, Morikawa T (1981) Preferential hydration of bovine serum albumin in polyhydric alcohol-water mixtures. J Biochem 90:39-50
    • (1981) J Biochem , vol.90 , pp. 39-50
    • Gekko, K.1    Morikawa, T.2
  • 5
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol - Preferential hydration in glycerol-water mixtures
    • 10.1021/bi00519a023
    • Gekko K, Timasheff SN (1981) Mechanism of protein stabilization by glycerol - preferential hydration in glycerol-water mixtures. Biochemistry 20:4667-4676
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 6
    • 22844449351 scopus 로고    scopus 로고
    • Application of immobilized enzyme reactor in on-line high performance liquid chromatography: A review
    • 10.1016/j.jchromb.2005.01.031
    • Girelli AM, Mattei E (2005) Application of immobilized enzyme reactor in on-line high performance liquid chromatography: a review. J Chromatogr B Analyt Technol Biomed Life Sci 819:3-16
    • (2005) J Chromatogr B Analyt Technol Biomed Life Sci , vol.819 , pp. 3-16
    • Girelli, A.M.1    Mattei, E.2
  • 7
    • 33747203770 scopus 로고    scopus 로고
    • Characteristics of a mesoporous silicate immobilized trypsin bioreactor in organic media
    • 10.1021/bp050334y
    • Goradia D, Cooney J, Hodnett BK, Magner E (2006) Characteristics of a mesoporous silicate immobilized trypsin bioreactor in organic media. Biotechnol Prog 22:1125-1131
    • (2006) Biotechnol Prog , vol.22 , pp. 1125-1131
    • Goradia, D.1    Cooney, J.2    Hodnett, B.K.3    Magner, E.4
  • 8
    • 0029902287 scopus 로고    scopus 로고
    • On protein denaturation in aqueous-organic mixtures but not in pure organic solvents
    • 10.1021/ja961869d
    • Griebenow K, Klibanov AM (1996) On protein denaturation in aqueous-organic mixtures but not in pure organic solvents. J Am Chem Soc 118:11695-11700
    • (1996) J Am Chem Soc , vol.118 , pp. 11695-11700
    • Griebenow, K.1    Klibanov, A.M.2
  • 9
    • 0347134475 scopus 로고    scopus 로고
    • Immobilized metal-ion chelating capillary microreactor for peptide mapping analysis of proteins by matrix assisted laser desorption/ionization-time of flight-mass spectrometry
    • 10.1002/elps.200305621
    • Guo Z, Xu SY, Lei ZD, Zou HF, Guo GC (2003) Immobilized metal-ion chelating capillary microreactor for peptide mapping analysis of proteins by matrix assisted laser desorption/ionization-time of flight-mass spectrometry. Electrophoresis 24:3633-3639
    • (2003) Electrophoresis , vol.24 , pp. 3633-3639
    • Guo, Z.1    Xu, S.Y.2    Lei, Z.D.3    Zou, H.F.4    Guo, G.C.5
  • 10
    • 0026517617 scopus 로고
    • Enzyme function in organic solvents
    • 10.1111/j.1432-1033.1992.tb19823.x
    • Gupta MN (1992) Enzyme function in organic solvents. Eur J Biochem 203:25-32
    • (1992) Eur J Biochem , vol.203 , pp. 25-32
    • Gupta, M.N.1
  • 11
    • 0025882622 scopus 로고
    • Denaturation capacity - A new quantitative criterion for selection of organic solvents as reaction media in biocatalysis
    • 10.1111/j.1432-1033.1991.tb15983.x
    • Khmelnitsky YL, Mozhaev VV, Belova AB, Sergeeva MV, Martinek K (1991) Denaturation capacity - a new quantitative criterion for selection of organic solvents as reaction media in biocatalysis. Eur J Biochem 198:31-41
    • (1991) Eur J Biochem , vol.198 , pp. 31-41
    • Khmelnitsky, Y.L.1    Mozhaev, V.V.2    Belova, A.B.3    Sergeeva, M.V.4    Martinek, K.5
  • 12
    • 0016022523 scopus 로고
    • Hydration of proteins and polypeptides
    • 10.1016/S0065-3233(08)60232-6
    • Kuntz ID, Kauzmann W (1974) Hydration of proteins and polypeptides. Adv Protein Chem 28:239-345
    • (1974) Adv Protein Chem , vol.28 , pp. 239-345
    • Kuntz, I.D.1    Kauzmann, W.2
  • 13
    • 85016229161 scopus 로고    scopus 로고
    • Large-scale protein identification using mass spectrometry
    • 10.1016/S1570-9639(02)00546-0
    • Lin D, Tabb DL, Yates JR (2003) Large-scale protein identification using mass spectrometry. Biochem Biophys Acta-Proteins Proteomics 1646:1-10
    • (2003) Biochem Biophys Acta-Proteins Proteomics , vol.1646 , pp. 1-10
    • Lin, D.1    Tabb, D.L.2    Yates, J.R.3
  • 14
    • 26844475051 scopus 로고    scopus 로고
    • Ultra fast trypsin digestion of proteins by high intensity focused ultrasound
    • 10.1021/pr050112v
    • Lopez-Ferrer D, Capelo JL, Vazquez J (2005) Ultra fast trypsin digestion of proteins by high intensity focused ultrasound. J Proteome Res 4:1569-1574
    • (2005) J Proteome Res , vol.4 , pp. 1569-1574
    • Lopez-Ferrer, D.1    Capelo, J.L.2    Vazquez, J.3
  • 17
    • 0034479737 scopus 로고    scopus 로고
    • Polyaniline: A conductive polymer coating for durable nanospray emitters
    • 10.1016/S1044-0305(00)00134-3
    • Maziarz EP, Lorenz SA, White TP, Wood TD (2000) Polyaniline: a conductive polymer coating for durable nanospray emitters. J Am Soc Mass Spectrom 11:659-663
    • (2000) J Am Soc Mass Spectrom , vol.11 , pp. 659-663
    • Maziarz, E.P.1    Lorenz, S.A.2    White, T.P.3    Wood, T.D.4
  • 19
    • 0035356739 scopus 로고    scopus 로고
    • Proteolysis in mixed organic-Aqueous solvent systems; Applications for peptide mass mapping using mass spectrometry
    • 10.1021/ac001332p
    • Russell WK, Park ZY, Russell DH (2001) Proteolysis in mixed organic-Aqueous solvent systems; applications for peptide mass mapping using mass spectrometry. Anal Chem 73:2682-2685
    • (2001) Anal Chem , vol.73 , pp. 2682-2685
    • Russell, W.K.1    Park, Z.Y.2    Russell, D.H.3
  • 20
    • 54349100675 scopus 로고    scopus 로고
    • An improved clean sonoreactor-based method for protein identification by mass spectrometry-based techniques
    • 10.1016/j.talanta.2008.07.048
    • Santos HM, Mota C, Lodeiro C, Moura I, Isaac I, Capelo JL (2008) An improved clean sonoreactor-based method for protein identification by mass spectrometry-based techniques. Talanta 77:870-875
    • (2008) Talanta , vol.77 , pp. 870-875
    • Santos, H.M.1    Mota, C.2    Lodeiro, C.3    Moura, I.4    Isaac, I.5    Capelo, J.L.6
  • 21
    • 1542652441 scopus 로고
    • A spectrophotometric determination of trypsin and chymotrypsin
    • 10.1016/0006-3002(55)90280-8
    • Schwert GW, Takenaka Y (1955) A spectrophotometric determination of trypsin and chymotrypsin. Biochim Biophys Acta 16:570-575
    • (1955) Biochim Biophys Acta , vol.16 , pp. 570-575
    • Schwert, G.W.1    Takenaka, Y.2
  • 22
    • 0027909392 scopus 로고
    • Comparison of soluble and immobilized trypsin kinetics: Implications for peptide synthesis
    • 10.1002/bit.260420116
    • Sears PS, Clark DS (1993) Comparison of soluble and immobilized trypsin kinetics: implications for peptide synthesis. Biotechnol Bioeng 42:118-124
    • (1993) Biotechnol Bioeng , vol.42 , pp. 118-124
    • Sears, P.S.1    Clark, D.S.2
  • 23
    • 0032472351 scopus 로고    scopus 로고
    • Stability of hydrolytic enzymes in water-organic solvent systems
    • 10.1016/S1381-1177(97)00019-2
    • Simon LM, Laszlo K, Vertesi A, Bagi K, Szajani B (1998) Stability of hydrolytic enzymes in water-organic solvent systems. J Mol Catal B-Enzym 4:41-45
    • (1998) J Mol Catal B-Enzym , vol.4 , pp. 41-45
    • Simon, L.M.1    Laszlo, K.2    Vertesi, A.3    Bagi, K.4    Szajani, B.5
  • 24
    • 30044447894 scopus 로고    scopus 로고
    • Efficient and specific trypsin digestion of microgram to nanogram quantities of proteins in organic-Aqueous solvent systems
    • 10.1021/ac051348l
    • Strader MB, Tabb DL, Hervey WJ, Pan CL, Hurst GB (2006) Efficient and specific trypsin digestion of microgram to nanogram quantities of proteins in organic-Aqueous solvent systems. Anal Chem 78:125-134
    • (2006) Anal Chem , vol.78 , pp. 125-134
    • Strader, M.B.1    Tabb, D.L.2    Hervey, W.J.3    Pan, C.L.4    Hurst, G.B.5
  • 26
    • 0015523063 scopus 로고
    • Enzymology in aqueous-organic cosolvent binary mixtures
    • Tan KH, Lovrien R (1972) Enzymology in aqueous-organic cosolvent binary mixtures. J Biol Chem 247:3278-3285
    • (1972) J Biol Chem , vol.247 , pp. 3278-3285
    • Tan, K.H.1    Lovrien, R.2
  • 27
    • 78649858218 scopus 로고    scopus 로고
    • Advances in proximal fluid proteomics for disease biomarker discovery
    • 10.1021/pr100904q
    • Teng PN, Bateman NW, Hood BL, Conrads TP (2010) Advances in proximal fluid proteomics for disease biomarker discovery. J Proteome Res 9:6091-6100
    • (2010) J Proteome Res , vol.9 , pp. 6091-6100
    • Teng, P.N.1    Bateman, N.W.2    Hood, B.L.3    Conrads, T.P.4
  • 29
    • 0035817408 scopus 로고    scopus 로고
    • Enzyme stabilization by covalent binding in nanoporous sol-gel glass for nonaqueous biocatalysis
    • 10.1002/bit.1114
    • Wang P, Dai S, Waezsada SD, Tsao AY, Davison BH (2001) Enzyme stabilization by covalent binding in nanoporous sol-gel glass for nonaqueous biocatalysis. Biotechnol Bioeng 74:249-255
    • (2001) Biotechnol Bioeng , vol.74 , pp. 249-255
    • Wang, P.1    Dai, S.2    Waezsada, S.D.3    Tsao, A.Y.4    Davison, B.H.5
  • 30
    • 0017285648 scopus 로고
    • Studies on immobilized trypsin in high concentrations of organic solvents
    • 10.1002/bit.260180109
    • Weetall HH, Vann WP (1976) Studies on immobilized trypsin in high concentrations of organic solvents. Biotechnol Bioeng 18:105-118
    • (1976) Biotechnol Bioeng , vol.18 , pp. 105-118
    • Weetall, H.H.1    Vann, W.P.2
  • 31
    • 0142224249 scopus 로고    scopus 로고
    • Reproducibility in fabrication and analytical performance of polyaniline-coated nanoelectrospray emitters
    • 10.1021/ac026446a
    • White TP, Wood TD (2003) Reproducibility in fabrication and analytical performance of polyaniline-coated nanoelectrospray emitters. Anal Chem 75:3660-3665
    • (2003) Anal Chem , vol.75 , pp. 3660-3665
    • White, T.P.1    Wood, T.D.2
  • 32
    • 10944274115 scopus 로고    scopus 로고
    • Enzymatic reaction of the immobilized enzyme on porous silicon studied by matrix-Assisted laser desorption/ionization-time of flight-mass spectrometry
    • 10.1002/elps.200406063
    • Xu SY, Pan CS, Hu LG, Zhang Z, Guo X, Zou HF (2004) Enzymatic reaction of the immobilized enzyme on porous silicon studied by matrix-Assisted laser desorption/ionization-time of flight-mass spectrometry. Electrophoresis 25:3669-3676
    • (2004) Electrophoresis , vol.25 , pp. 3669-3676
    • Xu, S.Y.1    Pan, C.S.2    Hu, L.G.3    Zhang, Z.4    Guo, X.5    Zou, H.F.6
  • 33
    • 33751534187 scopus 로고    scopus 로고
    • Integration of an on-line protein digestion microreactor to a nanoelectrospray emitter for peptide mapping
    • 10.1016/j.ab.2006.09.005
    • Zhao C, Jiang H, Smith DR, Bruckenstein S, Wood TD (2006) Integration of an on-line protein digestion microreactor to a nanoelectrospray emitter for peptide mapping. Anal Biochem 359:167-175
    • (2006) Anal Biochem , vol.359 , pp. 167-175
    • Zhao, C.1    Jiang, H.2    Smith, D.R.3    Bruckenstein, S.4    Wood, T.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.