메뉴 건너뛰기




Volumn 9, Issue 1, 2009, Pages 171-181

A dual fluorescent/MALDI chip platform for analyzing enzymatic activity and for protein profiling

Author keywords

Enzyme activity assay; Fluorescamine; Fluorescence screening; Pmaldi chip; Protease inhibitor

Indexed keywords

COPOLYMER; FLUORESCAMINE; PROTEINASE; PROTEINASE INHIBITOR; TRYPSIN; BOVINE SERUM ALBUMIN; PEPTIDE; PEPTIDE HYDROLASE; RIBULOSEBISPHOSPHATE CARBOXYLASE; VEGETABLE PROTEIN;

EID: 59449104400     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800390     Document Type: Article
Times cited : (8)

References (39)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry- based prote- omics
    • Aebersold, R., Mann, M., Mass spectrometry- based prote- omics. Nature 2003, 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI- quadrupole time-of-flight mass spec- trometry and BLAST homology searching
    • Shevchenko, A., Sunyaev, S., Loboda, A., Shevchenko, A. et al., Charting the proteomes of organisms with unsequenced genomes by MALDI- quadrupole time-of-flight mass spec- trometry and BLAST homology searching. Anal. Chem. 2001, 73, 1917-1926.
    • (2001) Anal. Chem , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Shevchenko, A.4
  • 3
    • 84984752764 scopus 로고    scopus 로고
    • Assignment of protein function in the postgenomic era
    • Saghatelian, A., Cravatt, B. F., Assignment of protein function in the postgenomic era. Nat. Chem. Biol. 2005, 1, 130-142.
    • (2005) Nat. Chem. Biol , vol.1 , pp. 130-142
    • Saghatelian, A.1    Cravatt, B.F.2
  • 4
    • 33646462162 scopus 로고    scopus 로고
    • Prote- omic profiling of metalloprotease activities with cocktails of active-site probes
    • Sieber, S. A., Niessen, S., Hoover, H. S., Cravatt, B. F., Prote- omic profiling of metalloprotease activities with cocktails of active-site probes. Nat. Chem. Biol. 2006, 2, 274-281.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 274-281
    • Sieber, S.A.1    Niessen, S.2    Hoover, H.S.3    Cravatt, B.F.4
  • 5
    • 12244253039 scopus 로고    scopus 로고
    • A high-throughput, low-volume enzyme assay on solid support
    • Babiak, P., Reymond, J. L., A high-throughput, low-volume enzyme assay on solid support. Anal. Chem. 2005, 77,373-377.
    • (2005) Anal. Chem , vol.77 , pp. 373-377
    • Babiak, P.1    Reymond, J.L.2
  • 6
    • 3242659948 scopus 로고    scopus 로고
    • A method for connecting solution-phase enzyme activity assays with immobilized format analysis by mass spectrometry
    • Min, D. H., Yeo, W. S., Mrksich, M., A method for connecting solution-phase enzyme activity assays with immobilized format analysis by mass spectrometry. Anal. Chem. 2004, 76, 3923-3929.
    • (2004) Anal. Chem , vol.76 , pp. 3923-3929
    • Min, D.H.1    Yeo, W.S.2    Mrksich, M.3
  • 7
    • 1542600384 scopus 로고    scopus 로고
    • Detection of protease activities with the mass-spectrometry- assisted enzyme-screening (MES) system
    • Schluter, H., Jankowski, J., Rykl, J., Thiemann, J. et al., Detection of protease activities with the mass-spectrometry- assisted enzyme-screening (MES) system. Anal. Bioanal. Chem. 2003, 377, 1102-1107.
    • (2003) Anal. Bioanal. Chem , vol.377 , pp. 1102-1107
    • Schluter, H.1    Jankowski, J.2    Rykl, J.3    Thiemann, J.4
  • 8
    • 7044237454 scopus 로고    scopus 로고
    • Integrated protein microchip assay with dual fluorescent- and MALDI read-out
    • Finnskog, D., Ressine, A., Laurell, T., Marko-Varga, G., Integrated protein microchip assay with dual fluorescent- and MALDI read-out. J. Proteome Res. 2004, 3, 988-994.
    • (2004) J. Proteome Res , vol.3 , pp. 988-994
    • Finnskog, D.1    Ressine, A.2    Laurell, T.3    Marko-Varga, G.4
  • 9
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10000 daltons
    • Karas, M., Hillenkamp, F., Laser desorption ionization of proteins with molecular masses exceeding 10000 daltons. Anal. Chem. 1988, 60, 2299-2301.
    • (1988) Anal. Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 10
    • 0034761614 scopus 로고    scopus 로고
    • Disposable polymeric high-density nanovial arrays for matrix assisted laser desorption / ionization- time of flight-mass spectrometry: II. Biological applications
    • Ekstrom, S., Nilsson, J., Helldin, G., Laurell, T. et al., Disposable polymeric high-density nanovial arrays for matrix assisted laser desorption / ionization- time of flight-mass spectrometry: II. Biological applications. Electrophoresis 2001, 22, 3984-3992.
    • (2001) Electrophoresis , vol.22 , pp. 3984-3992
    • Ekstrom, S.1    Nilsson, J.2    Helldin, G.3    Laurell, T.4
  • 11
    • 59549104137 scopus 로고    scopus 로고
    • Retentate chromatography and protein chip arrays with application in biology and medicine.
    • United States Patent 0123043 A1, 2002
    • Hutchens, T., Yip, T. T., Retentate chromatography and protein chip arrays with application in biology and medicine. United States Patent 0123043 A1, 2002.
    • Hutchens, T.1    Yip, T.T.2
  • 12
    • 0034755602 scopus 로고    scopus 로고
    • Disposable polymeric high-density nanovial arrays for matrix assisted laser desorption / ionization-time of flight- mass spectrometry: I. Microstructure development and manufacturing
    • Marko-Varga, G., Ekstrom, S., Heildin, G., Nilsson, J. et al., Disposable polymeric high-density nanovial arrays for matrix assisted laser desorption / ionization-time of flight- mass spectrometry: I. Microstructure development and manufacturing. Electrophoresis 2001, 22, 3978-3983.
    • (2001) Electrophoresis , vol.22 , pp. 3978-3983
    • Marko-Varga, G.1    Ekstrom, S.2    Heildin, G.3    Nilsson, J.4
  • 13
    • 59549095143 scopus 로고    scopus 로고
    • Structured biosample support plates for mass spectroscopic analyses and procedures for manufacturing and use.
    • United States Patent 0045270 A1, 2002
    • Schurenberg, M., Franzen, J, Structured biosample support plates for mass spectroscopic analyses and procedures for manufacturing and use. United States Patent 0045270 A1, 2002.
    • Schurenberg, M.1    Franzen, J.2
  • 15
    • 23144432648 scopus 로고    scopus 로고
    • Fast prototyping of hydrophobic disposable polymer support arrays for matrix-assisted laser desorption/ ionization- time of flight-mass spectrometry of proteins by atmospheric molding
    • Muck, A., Nesnerova, P., Pichova, I., Svatos, A., Fast prototyping of hydrophobic disposable polymer support arrays for matrix-assisted laser desorption/ ionization- time of flight-mass spectrometry of proteins by atmospheric molding. Electrophoresis 2005, 26, 2835-2842.
    • (2005) Electrophoresis , vol.26 , pp. 2835-2842
    • Muck, A.1    Nesnerova, P.2    Pichova, I.3    Svatos, A.4
  • 16
    • 0001144526 scopus 로고
    • Seed storage proteins: The enzyme inhibitors
    • Richardson, M., Seed storage proteins: The enzyme inhibitors. Meth. Plant Biochem. 1991, 5, 259-305.
    • (1991) Meth. Plant Biochem , vol.5 , pp. 259-305
    • Richardson, M.1
  • 18
    • 0015592078 scopus 로고
    • Amino acid analysis with fluorescamine at the picomole level
    • Stein, S., Bohlen, P., Stone, J., Dairman, W. et al., Amino acid analysis with fluorescamine at the picomole level. Arch. Biochem. Biophys. 1973, 155, 202-212.
    • (1973) Arch. Biochem. Biophys , vol.155 , pp. 202-212
    • Stein, S.1    Bohlen, P.2    Stone, J.3    Dairman, W.4
  • 19
    • 0015522277 scopus 로고
    • Fluorescamine: A reagent for assay of amino acids, pep- tides, proteins, and primary amines in the picomole range
    • Udenfriend, S., Stein, S., Bohlen, P., Dairman, W. et al., Fluorescamine: A reagent for assay of amino acids, pep- tides, proteins, and primary amines in the picomole range. Science 1972, 178, 871-872.
    • (1972) Science , vol.178 , pp. 871-872
    • Udenfriend, S.1    Stein, S.2    Bohlen, P.3    Dairman, W.4
  • 21
    • 0029257325 scopus 로고
    • Errors and artifacts in coupled spectro- photometric assays of enzyme activity
    • Kruger, N. J., Errors and artifacts in coupled spectro- photometric assays of enzyme activity. Phytochemistry 1995, 38, 1065-1071.
    • (1995) Phytochemistry , vol.38 , pp. 1065-1071
    • Kruger, N.J.1
  • 22
    • 39149095322 scopus 로고    scopus 로고
    • A mass spectrometry-based strategy for detecting and characterizing endogenous proteinase activities in complex biological samples
    • Robinson, S., Niles, R. K., Witkowska, H. E., Rittenbach, K. J. et al., A mass spectrometry-based strategy for detecting and characterizing endogenous proteinase activities in complex biological samples. Proteomics 2008, 8, 435-445.
    • (2008) Proteomics , vol.8 , pp. 435-445
    • Robinson, S.1    Niles, R.K.2    Witkowska, H.E.3    Rittenbach, K.J.4
  • 23
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: Genes for improving defenses against insects and pathogens
    • Ryan, C., Protease inhibitors in plants: Genes for improving defenses against insects and pathogens. Annu. Rev. Phyto- pathol. 1990, 28, 425-449.
    • (1990) Annu. Rev. Phyto- pathol , vol.28 , pp. 425-449
    • Ryan, C.1
  • 24
    • 0027605348 scopus 로고
    • Purification and characterization from tobacco (Nicotiana tabacum) leaves of six small, wound-inducible, proteinase isoinhibitors of the potato inhibitor II family
    • Pearce, G., Johnson, S., Ryan, C. A., Purification and characterization from tobacco (Nicotiana tabacum) leaves of six small, wound-inducible, proteinase isoinhibitors of the potato inhibitor II family. Plant Physiol. 1993, 102, 639-644.
    • (1993) Plant Physiol , vol.102 , pp. 639-644
    • Pearce, G.1    Johnson, S.2    Ryan, C.A.3
  • 25
    • 0027551083 scopus 로고
    • Proteinase inhibitors in Nicotiana alata stigmas are derived from a precursor protein which is processed into five homologous inhibitors
    • Atkinson, A. H., Heath, R. L., Simpson, R. J., Clarke, A. E. et al., Proteinase inhibitors in Nicotiana alata stigmas are derived from a precursor protein which is processed into five homologous inhibitors. Plant Cell 1993, 5, 203-213.
    • (1993) Plant Cell , vol.5 , pp. 203-213
    • Atkinson, A.H.1    Heath, R.L.2    Simpson, R.J.3    Clarke, A.E.4
  • 26
    • 0035543848 scopus 로고    scopus 로고
    • A protein- ase inhibitor II of Solanum americanum is expressed in phloem
    • Xu, Z. F., Qi, W. Q., Ouyang, X. Z., Yeung, E. etal., A protein- ase inhibitor II of Solanum americanum is expressed in phloem. Plant Mol. Biol. 2001, 47, 727-738.
    • (2001) Plant Mol. Biol , vol.47 , pp. 727-738
    • Xu, Z.F.1    Qi, W.Q.2    Ouyang, X.Z.3    Yeung, E.4
  • 27
    • 0033017462 scopus 로고    scopus 로고
    • A novel two-chain proteinase inhibitor generated by circular- ization of a multidomain precursor protein
    • Lee, M. C., Scanlon, M. J., Craik, D. J., Anderson, M. A., A novel two-chain proteinase inhibitor generated by circular- ization of a multidomain precursor protein. Nat. Struct. Biol. 1999, 6, 526-530.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 526-530
    • Lee, M.C.1    Scanlon, M.J.2    Craik, D.J.3    Anderson, M.A.4
  • 28
    • 33644795085 scopus 로고    scopus 로고
    • Differential elicitation of two processing proteases controls the processing pattern of the trypsin proteinase inhibitor precursor in Nicotiana attenuata
    • Horn, M., Patankar, A. G., Zavala, J. A., Wu, J. etal., Differential elicitation of two processing proteases controls the processing pattern of the trypsin proteinase inhibitor precursor in Nicotiana attenuata. Plant Physiol. 2005, 139, 375-388.
    • (2005) Plant Physiol , vol.139 , pp. 375-388
    • Horn, M.1    Patankar, A.G.2    Zavala, J.A.3    Wu, J.4
  • 29
    • 0014099225 scopus 로고
    • Quantitative determination of soluble cellular proteins by radial diffusion in agar gels containing antibodies
    • Ryan, C. A., Quantitative determination of soluble cellular proteins by radial diffusion in agar gels containing antibodies. Anal. Biochem. 1967, 19, 434-440.
    • (1967) Anal. Biochem , vol.19 , pp. 434-440
    • Ryan, C.A.1
  • 30
    • 0027220491 scopus 로고
    • Quantitative determination of serine proteinase inhibitor activity using a radial diffusion assay
    • Jongsma, M. A., Bakker, P. L., Stiekema, W. J., Quantitative determination of serine proteinase inhibitor activity using a radial diffusion assay. Anal. Biochem. 1993, 212, 79-84.
    • (1993) Anal. Biochem , vol.212 , pp. 79-84
    • Jongsma, M.A.1    Bakker, P.L.2    Stiekema, W.J.3
  • 31
    • 1942517968 scopus 로고    scopus 로고
    • Solanum nigrum: A model ecological expression system and its tools
    • Schmidt, D. D., Kessler, A., Kessler, D., Schmidt, S. et al., Solanum nigrum: A model ecological expression system and its tools. Mol. Ecol. 2004, 13, 981-995.
    • (2004) Mol. Ecol , vol.13 , pp. 981-995
    • Schmidt, D.D.1    Kessler, A.2    Kessler, D.3    Schmidt, S.4
  • 32
    • 33947604551 scopus 로고    scopus 로고
    • Trypsin- linked copolymer MALDI chips for fast protein identification
    • Ibanez, A. J., Muck, A., Halim, V., Svatos, A., Trypsin- linked copolymer MALDI chips for fast protein identification. J. Proteome Res. 2007, 6, 1183-1189.
    • (2007) J. Proteome Res , vol.6 , pp. 1183-1189
    • Ibanez, A.J.1    Muck, A.2    Halim, V.3    Svatos, A.4
  • 33
    • 85115449762 scopus 로고    scopus 로고
    • Schmidt, S., Baldwin, I. T., Systemin in Solanum nigrum. The tomato-homologous polypeptide does not mediate direct defense responses. Plant Physiol. 2006, 142, 1751-1758.
    • Schmidt, S., Baldwin, I. T., Systemin in Solanum nigrum. The tomato-homologous polypeptide does not mediate direct defense responses. Plant Physiol. 2006, 142, 1751-1758.
  • 34
    • 0028310026 scopus 로고
    • Trypsin inhibitor activity in mature tobacco and tomato plants is mainly induced locally in response to insect attact, wounding and virus infection
    • Jongsma, M. A., Bakker, P. L., Visser, B., Stiekema, W. J., Trypsin inhibitor activity in mature tobacco and tomato plants is mainly induced locally in response to insect attact, wounding and virus infection. Planta 1994, 195, 29-35.
    • (1994) Planta , vol.195 , pp. 29-35
    • Jongsma, M.A.1    Bakker, P.L.2    Visser, B.3    Stiekema, W.J.4
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 10944272148 scopus 로고    scopus 로고
    • Cloning and characterization of chymotrypsin- and trypsin- like cDNAs from the gut of the Hessian fly (Mayetiola destructor (Say))
    • Zhu, Y. C., Liu, X., Maddur, A. A., Oppert, B. et al., Cloning and characterization of chymotrypsin- and trypsin- like cDNAs from the gut of the Hessian fly (Mayetiola destructor (Say)). Insect Biochem. Mol. Biol. 2005, 35, 23-32.
    • (2005) Insect Biochem. Mol. Biol , vol.35 , pp. 23-32
    • Zhu, Y.C.1    Liu, X.2    Maddur, A.A.3    Oppert, B.4
  • 37
    • 33845975973 scopus 로고    scopus 로고
    • Atmospheric molding of ionic copolymer MALDI-TOF/MS arrays: A new tool for protein identification/profiling
    • Muck, A., Ibanez, A. J., Stauber, E. J., Mansourova, M. et al., Atmospheric molding of ionic copolymer MALDI-TOF/MS arrays: A new tool for protein identification/profiling. Elec- trophoresis 2006, 27, 4952-4959.
    • (2006) Elec- trophoresis , vol.27 , pp. 4952-4959
    • Muck, A.1    Ibanez, A.J.2    Stauber, E.J.3    Mansourova, M.4
  • 38
    • 1442323792 scopus 로고    scopus 로고
    • Quantitative matrix- assisted laser desorption/ionization mass spectrometry for the determination of enzyme activities
    • Bungert, D., Heinzle, E., Tholey, A., Quantitative matrix- assisted laser desorption/ionization mass spectrometry for the determination of enzyme activities. Anal. Biochem. 2004, 326, 167-175.
    • (2004) Anal. Biochem , vol.326 , pp. 167-175
    • Bungert, D.1    Heinzle, E.2    Tholey, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.