메뉴 건너뛰기




Volumn 10, Issue 16, 2010, Pages 2942-2949

Proteolysis approach without chemical modification for a simple and rapid analysis of disulfide bonds using thermostable protease-immobilized microreactors

Author keywords

Disulfide bond; Enzyme immobilization; Protease; Proteolysis; Technology; Thermal denaturation

Indexed keywords

LYSOZYME; PROTEINASE;

EID: 77955598985     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000166     Document Type: Article
Times cited : (7)

References (23)
  • 1
    • 1342304902 scopus 로고    scopus 로고
    • Defining the plant disulfide proteome
    • Lee, K., Lee, J., Kim, Y., Bae, D. et al., Defining the plant disulfide proteome. Electrophoresis 2004, 25, 532-541.
    • (2004) Electrophoresis , vol.25 , pp. 532-541
    • Lee, K.1    Lee, J.2    Kim, Y.3    Bae, D.4
  • 2
    • 53049102637 scopus 로고    scopus 로고
    • Introduction of the disulfide proteome: Application of a technique for the analysis of plant storage proteins as well as allergens
    • Yano, H., Kuroda, S., Introduction of the disulfide proteome: application of a technique for the analysis of plant storage proteins as well as allergens. J. Proteome Res. 2008, 7, 3071-3079.
    • (2008) J. Proteome Res. , vol.7 , pp. 3071-3079
    • Yano, H.1    Kuroda, S.2
  • 3
    • 51349088530 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical implications of reversible protein S-glutathionylation
    • Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A., Shelton, M. D., Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid. Redox Signal. 2008, 10, 1941-1988.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1941-1988
    • Mieyal, J.J.1    Gallogly, M.M.2    Qanungo, S.3    Sabens, E.A.4    Shelton, M.D.5
  • 4
    • 0037085393 scopus 로고    scopus 로고
    • Disulfide bond assignments of secreted Frizzled-related protein-1 provide insights about Frizzled homology and netrin modules
    • DOI 10.1074/jbc.M108533200
    • Chong, J. M., Üren, A., Rubin, J. S., Speicher, D. W., Disulfide bond assignments of secreted Frizzled-related protein-1 provide insights about Frizzled homology and netrin modules. J. Biol. Chem. 2002, 277, 5134-5144. (Pubitemid 34968556)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.7 , pp. 5134-5144
    • Chong, J.M.1    Uren, A.2    Rubin, J.S.3    Speicher, D.W.4
  • 5
    • 0346220263 scopus 로고    scopus 로고
    • Disulfide mapping of the cyclotide kalata B1
    • Göransson, U., Craik, D. J., Disulfide mapping of the cyclotide kalata B1. J. Biol. Chem. 2003, 278, 48186-48196.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48186-48196
    • Göransson, U.1    Craik, D.J.2
  • 6
    • 75149168873 scopus 로고    scopus 로고
    • Synthesis and disulfide bond connectivity-activity studies of a kalata B1-inspired cyclopeptide against dengue NS2B-NS3 protease
    • Gao, Y., Cui, T., Lam, Y., Synthesis and disulfide bond connectivity-activity studies of a kalata B1-inspired cyclopeptide against dengue NS2B-NS3 protease. Bioorg. Med. Chem. 2010, 18, 1331-1336.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 1331-1336
    • Gao, Y.1    Cui, T.2    Lam, Y.3
  • 8
    • 36949013412 scopus 로고    scopus 로고
    • Monolith-based immobilized enzyme reactors: Recent developments and applications for proteome analysis
    • DOI 10.1002/jssc.200700362
    • Ma, J., Zhang, L., Liang, Z., Zhang, W., Zhang, Y., Monolith-based immobilized enzyme reactors: recent developments and applications for proteome analysis. J. Sep. Sci. 2007, 30, 3050-3059. (Pubitemid 350238340)
    • (2007) Journal of Separation Science , vol.30 , Issue.17 , pp. 3050-3059
    • Ma, J.1    Zhang, L.2    Liang, Z.3    Zhang, W.4    Zhang, Y.5
  • 9
    • 57649089547 scopus 로고    scopus 로고
    • Recent advance in immobilized enzymatic reactors and their applications in proteome analysis
    • Ma, J., Zhang, L., Liang, Z., Zhang, W., Zhang, Y., Recent advance in immobilized enzymatic reactors and their applications in proteome analysis. Anal. Chim. Acta 2009, 632, 1-8.
    • (2009) Anal. Chim. Acta , vol.632 , pp. 1-8
    • Ma, J.1    Zhang, L.2    Liang, Z.3    Zhang, W.4    Zhang, Y.5
  • 10
    • 68749110902 scopus 로고    scopus 로고
    • Microfluidics with MALDI analysis for proteomics - A review
    • Lee, J., Soper, S. A., Murray, K. K.,Microfluidics with MALDI analysis for proteomics - a review. Anal. Chim. Acta 2009, 649, 180-190.
    • (2009) Anal. Chim. Acta , vol.649 , pp. 180-190
    • Lee, J.1    Soper, S.A.2    Murray, K.K.3
  • 11
    • 27644480768 scopus 로고    scopus 로고
    • Immobilization of enzymes on a microchannel surface through cross-linking polymerization
    • DOI 10.1039/b510605b
    • Honda, T., Miyazaki, M., Nakamura, H., Maeda, H., Immobilization of enzymes on a microchannel surface through cross-linking polymerization. Chem. Commun. 2005, 5062-5064. (Pubitemid 41566433)
    • (2005) Chemical Communications , Issue.40 , pp. 5062-5064
    • Honda, T.1    Miyazaki, M.2    Nakamura, H.3    Maeda, H.4
  • 12
    • 33750524054 scopus 로고    scopus 로고
    • Facile preparation of an enzyme-immobilized microreactor using a cross-linking enzyme membrane on a microchannel surface
    • DOI 10.1002/adsc.200606224
    • Honda, T., Miyazaki, M., Nakamura, H., Maeda, H., Facile preparation of an enzyme-immobilized microreactor using a cross-linking enzyme membrane on a microchannel surface. Adv. Synth. Catal. 2006, 348, 2163-2171. (Pubitemid 44662644)
    • (2006) Advanced Synthesis and Catalysis , vol.348 , Issue.15 , pp. 2163-2171
    • Honda, T.1    Miyazaki, M.2    Nakamura, H.3    Maeda, H.4
  • 13
    • 70449876733 scopus 로고    scopus 로고
    • Rapid and efficient proteolysis for proteomic analysis by protease-immobilized microreactor
    • Yamaguchi, H., Miyazaki, M., Honda, T., Briones-Nagata, M. P. et al., Rapid and efficient proteolysis for proteomic analysis by protease-immobilized microreactor. Electrophoresis 2009, 30, 3257-3264.
    • (2009) Electrophoresis , vol.30 , pp. 3257-3264
    • Yamaguchi, H.1    Miyazaki, M.2    Honda, T.3    Briones-Nagata, M.P.4
  • 14
    • 0034212611 scopus 로고    scopus 로고
    • Thermal denaturation: A useful technique in peptide mass mapping
    • Park, Z.-Y., Russell, D. H., Thermal denaturation: a useful technique in peptide mass mapping. Anal. Chem. 2000, 72, 2667-2670.
    • (2000) Anal. Chem. , vol.72 , pp. 2667-2670
    • Park, Z.-Y.1    Russell, D.H.2
  • 15
    • 33746537155 scopus 로고    scopus 로고
    • Application of a temperature-controllable microreactor to simple and rapid protein identification using MALDI-TOF MS
    • Sim, T. S., Kim, E.-M., Joo, H. S., Kim, B. G., Kim, Y.-K., Application of a temperature-controllable microreactor to simple and rapid protein identification using MALDI-TOF MS. Lab. Chip 2006, 6, 1056-1061.
    • (2006) Lab. Chip , vol.6 , pp. 1056-1061
    • Sim, T.S.1    Kim, E.-M.2    Joo, H.S.3    Kim, B.G.4    Kim, Y.-K.5
  • 16
    • 70449848012 scopus 로고    scopus 로고
    • Integration of electrodes in a suction cup-driven microchip for alternating current-accelerated proteolysis
    • Liu, T., Bao, H., Zhang, L., Chen, G., Integration of electrodes in a suction cup-driven microchip for alternating current-accelerated proteolysis. Electrophoresis 2009, 30, 3265-3268.
    • (2009) Electrophoresis , vol.30 , pp. 3265-3268
    • Liu, T.1    Bao, H.2    Zhang, L.3    Chen, G.4
  • 17
    • 34948845083 scopus 로고    scopus 로고
    • Immobilization of trypsin on superparamagnetic nanoparticles for rapid and effective proteolysis
    • DOI 10.1021/pr070132s
    • Li, Y., Xu, X., Deng, C., Yang, P., Zhang, X., Immobilization of trypsin on superparamagnetic nanoparticles for rapid and effective proteolysis. J. Proteome Res. 2007, 6, 3849-3855. (Pubitemid 47522774)
    • (2007) Journal of Proteome Research , vol.6 , Issue.9 , pp. 3849-3855
    • Li, Y.1    Xu, X.2    Deng, C.3    Yang, P.4    Zhang, X.5
  • 18
    • 77749345719 scopus 로고    scopus 로고
    • Integration of protein processing steps on a droplet microfluidics platform for MALDI-MS analysis
    • Chatterjee, D., Ytterberg, A. J., Son, S. U., Loo, J. A., Garrell, R. L., Integration of protein processing steps on a droplet microfluidics platform for MALDI-MS analysis. Anal. Chem. 2010, 82, 2095-2101.
    • (2010) Anal. Chem. , vol.82 , pp. 2095-2101
    • Chatterjee, D.1    Ytterberg, A.J.2    Son, S.U.3    Loo, J.A.4    Garrell, R.L.5
  • 19
    • 42349103426 scopus 로고    scopus 로고
    • Organic-inorganic hybrid silica monolith based immobilized trypsin reactor with high enzymatic activity
    • DOI 10.1021/ac702343a
    • Ma, J., Liang,Z., Qiao, X., Deng, Q. et al., Organic-inorganic hybrid silica monolith based immobilized trypsin reactor with high enzymatic activity. Anal. Chem. 2008, 80, 2949-2956. (Pubitemid 351556460)
    • (2008) Analytical Chemistry , vol.80 , Issue.8 , pp. 2949-2956
    • Ma, J.1    Liang, Z.2    Qiao, X.3    Deng, Q.4    Tao, D.5    Zhang, L.6    Zhang, Y.7
  • 20
    • 0036646541 scopus 로고    scopus 로고
    • On-line trypsin-encapsulated enzyme reactor by the sol-gel method integrated into capillary electrophoresis
    • DOI 10.1021/ac0200421
    • Sakai-Kato, K., Kato, M., Toyooka, T., On-line trypsin-encapsulated enzyme reactor by the sol-gel method integrated into capillary electrophoresis. Anal. Chem. 2002, 74, 2943-2949. (Pubitemid 34755206)
    • (2002) Analytical Chemistry , vol.74 , Issue.13 , pp. 2943-2949
    • Sakai-Kato, K.1    Kato, M.2    Toyo'Oka, T.3
  • 21
    • 65349150524 scopus 로고    scopus 로고
    • Highly stable trypsin-aggregate coatings on polymer nanofibers for repeated protein digestion
    • Kim, B. C., Lopez-Ferrer, D., Lee, S.-M., Ahn, H.-K. et al., Highly stable trypsin-aggregate coatings on polymer nanofibers for repeated protein digestion. Proteomics 2009, 9, 1893-1900.
    • (2009) Proteomics , vol.9 , pp. 1893-1900
    • Kim, B.C.1    Lopez-Ferrer, D.2    Lee, S.-M.3    Ahn, H.-K.4
  • 22
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., Mann, M., Mass spectrometry-based proteomics. Nature 2003, 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 23
    • 35848970747 scopus 로고    scopus 로고
    • Mapping protein post-translational modifications with mass spectrometry
    • DOI 10.1038/nmeth1100, PII NMETH1100
    • Witze, E. S., Old, W. N., Resing, K. A., Ahn, N. G., Mapping protein post-translational modifications with mass spectrometry. Nat. Methods 2007, 10, 798-806. (Pubitemid 350055576)
    • (2007) Nature Methods , vol.4 , Issue.10 , pp. 798-806
    • Witze, E.S.1    Old, W.M.2    Resing, K.A.3    Ahn, N.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.