메뉴 건너뛰기




Volumn 8, Issue 7, 2009, Pages 3588-3597

Comparison between the matrices α-cyano-4-hydroxycinnamic acid and 4-chloro-α-cyanocinnamic acid for trypsin, chymotrypsin, and pepsin digestions by MALDI-TOF mass spectrometry

Author keywords

Charge state; CHCA; Chymotrypsin; Cl CCA; ClCCA; HCCA; Pepsin; Phosphorylation; pI; PMF; Protease; Proton affinity; Trypsin

Indexed keywords

4 CHLORO ALPHA CYANOCINNAMIC ACID; ALPHA CYANO 4 HYDROXYCINNAMIC ACID; CHYMOTRYPSIN; CINNAMIC ACID DERIVATIVE; PEPSIN A; TRYPSIN; UNCLASSIFIED DRUG;

EID: 67650394372     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr900274s     Document Type: Article
Times cited : (28)

References (33)
  • 1
    • 33845379876 scopus 로고
    • The influence of the wavelength in high irradiance ultraviolet laser desorption mass spectrometry of organic molecules
    • Karas, M.; Bachmann, D.; Hillenkamp, F. The influence of the wavelength in high irradiance ultraviolet laser desorption mass spectrometry of organic molecules. Anal. Chem. 1985, 57, 2935-2939.
    • (1985) Anal. Chem , vol.57 , pp. 2935-2939
    • Karas, M.1    Bachmann, D.2    Hillenkamp, F.3
  • 3
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 Da
    • Karas, M.; Hillenkamp, F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 Da. Anal. Chem. 1988, 60, 2299-2301.
    • (1988) Anal. Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 4
    • 0042386240 scopus 로고    scopus 로고
    • Protein identification: The origins of peptide mass fingerprinting
    • Henzel, W. J.; Watanabe, C.; Stults, J. T. Protein identification: The origins of peptide mass fingerprinting. J. Am. Soc. Mass Spectrom. 2003, 14, 931-942.
    • (2003) J. Am. Soc. Mass Spectrom , vol.14 , pp. 931-942
    • Henzel, W.J.1    Watanabe, C.2    Stults, J.T.3
  • 5
    • 0026811273 scopus 로고
    • Peptide sequencing by matrix assisted laser desorption mass spectrometry
    • Spengler, B.; Kirsch, D.; Kaufmann, R.; Jaeger, E. Peptide sequencing by matrix assisted laser desorption mass spectrometry. Rapid Commun. Mass Spectrom. 1992, 6, 105-108.
    • (1992) Rapid Commun. Mass Spectrom , vol.6 , pp. 105-108
    • Spengler, B.1    Kirsch, D.2    Kaufmann, R.3    Jaeger, E.4
  • 6
    • 0017056107 scopus 로고
    • Specificity of trypsin and alpha-chymotrypsin towards neutral substrates
    • Vajda, T.; Szabó, T. Specificity of trypsin and alpha-chymotrypsin towards neutral substrates. Acta Biochim. Biophys. Acad. Sci. Hung. 1976, 11, 287-294.
    • (1976) Acta Biochim. Biophys. Acad. Sci. Hung , vol.11 , pp. 287-294
    • Vajda, T.1    Szabó, T.2
  • 8
    • 0242386421 scopus 로고    scopus 로고
    • Use of different proteases working in acidic conditions to improve sequence coverage and resolution in hydrogen/deuterium exchange of large proteins
    • Cravello, L.; Lascoux, D.; Forest, E. Use of different proteases working in acidic conditions to improve sequence coverage and resolution in hydrogen/deuterium exchange of large proteins. Rapid Commun. Mass Spectrom. 2003, 17, 2387-2393.
    • (2003) Rapid Commun. Mass Spectrom , vol.17 , pp. 2387-2393
    • Cravello, L.1    Lascoux, D.2    Forest, E.3
  • 9
    • 26844537015 scopus 로고    scopus 로고
    • Complementary mass spectrometric techniques to achieve complete sequence coverage of recombinant human tropoelastin
    • Getie, M.; Schmelzer, C. E. H.; Weiss, A. S.; Neubert, R. H. H. Complementary mass spectrometric techniques to achieve complete sequence coverage of recombinant human tropoelastin. Rapid Commun. Mass Spectrom. 2005, 19, 2989-2993.
    • (2005) Rapid Commun. Mass Spectrom , vol.19 , pp. 2989-2993
    • Getie, M.1    Schmelzer, C.E.H.2    Weiss, A.S.3    Neubert, R.H.H.4
  • 10
    • 0013470971 scopus 로고
    • The multiple specificity of chymotrypsin
    • Fruton, J. S.; Bergmann, M. J. The multiple specificity of chymotrypsin. J. Biol. Chem. 1942, 145, 253-265.
    • (1942) J. Biol. Chem , vol.145 , pp. 253-265
    • Fruton, J.S.1    Bergmann, M.J.2
  • 11
    • 0013471212 scopus 로고    scopus 로고
    • Fruton, J. S. Specificity of chymotrypsin B. J. Biol. Chem. 1948, 173, 109-110.
    • Fruton, J. S. Specificity of chymotrypsin B. J. Biol. Chem. 1948, 173, 109-110.
  • 12
    • 0009459282 scopus 로고
    • The specificity of pepsin action
    • Fruton, J. S.; Bergmann, M. The specificity of pepsin action. Science 1938, 87, 557.
    • (1938) Science , vol.87 , pp. 557
    • Fruton, J.S.1    Bergmann, M.2
  • 13
    • 0041101623 scopus 로고
    • Specificity of pepsin and its dependence on a possible 'hydrophobic binding site'
    • Tang, J. Specificity of pepsin and its dependence on a possible 'hydrophobic binding site'. Nature 1963, 199, 1094-1095.
    • (1963) Nature , vol.199 , pp. 1094-1095
    • Tang, J.1
  • 16
    • 33646557331 scopus 로고    scopus 로고
    • Protein cleavage strategies for an improved analysis of the membrane proteome
    • Fischer, F.; Poetsch, A. Protein cleavage strategies for an improved analysis of the membrane proteome. Proteome Sci. 2006, 4, 1-12.
    • (2006) Proteome Sci , vol.4 , pp. 1-12
    • Fischer, F.1    Poetsch, A.2
  • 17
    • 0033214277 scopus 로고    scopus 로고
    • The dominance of arginine-containing peptides in MALDI-derived tryptic mass fingerprints of proteins
    • Krause, E.; Wenschuh, H.; Jungblut, P. R. The dominance of arginine-containing peptides in MALDI-derived tryptic mass fingerprints of proteins. Anal. Chem. 1999, 71, 4160-4165.
    • (1999) Anal. Chem , vol.71 , pp. 4160-4165
    • Krause, E.1    Wenschuh, H.2    Jungblut, P.R.3
  • 18
    • 50449099939 scopus 로고    scopus 로고
    • 4-Chloro-α-cyanocinnamic acid is an advanced, rationally designed MALDI matrix
    • Jaskolla, T. W.; Lehmann, W. D.; Karas, M. 4-Chloro-α-cyanocinnamic acid is an advanced, rationally designed MALDI matrix. Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 12200-12205.
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 12200-12205
    • Jaskolla, T.W.1    Lehmann, W.D.2    Karas, M.3
  • 19
    • 84989052470 scopus 로고
    • α-Cyano-4- hydroxycinnamic acid as a matrix for matrix-assisted laser desorption mass spectrometry
    • Beavis, R. C.; Chaudhary, T.; Chait, B. T. α-Cyano-4- hydroxycinnamic acid as a matrix for matrix-assisted laser desorption mass spectrometry. Org. Mass Spectrom. 1992, 27, 156-158.
    • (1992) Org. Mass Spectrom , vol.27 , pp. 156-158
    • Beavis, R.C.1    Chaudhary, T.2    Chait, B.T.3
  • 20
    • 0035997277 scopus 로고    scopus 로고
    • Identification of protein phosphorylation sites by combination of elastase digestion, immobilized metal affinity chromatography, and quadrupole-time of flight tandem mass spectrometry
    • Schlosser, A.; Bodem, J.; Bossemeyer, D.; Grummt, I.; Lehmann, W. D. Identification of protein phosphorylation sites by combination of elastase digestion, immobilized metal affinity chromatography, and quadrupole-time of flight tandem mass spectrometry. Proteomics 2002, 2, 911-918.
    • (2002) Proteomics , vol.2 , pp. 911-918
    • Schlosser, A.1    Bodem, J.2    Bossemeyer, D.3    Grummt, I.4    Lehmann, W.D.5
  • 21
    • 64049088118 scopus 로고    scopus 로고
    • The new matrix 4-chloro-α-cyanocinnamic acid allows the detection of phosphatidylethanolamine chloramines by MALDI-TOF mass spectrometry
    • Jaskolla, T. W.; Fuchs, B.; Karas, M.; Schiller, J. The new matrix 4-chloro-α-cyanocinnamic acid allows the detection of phosphatidylethanolamine chloramines by MALDI-TOF mass spectrometry. J. Am. Soc. Mass Spectrom. 2009, 20, 867-874.
    • (2009) J. Am. Soc. Mass Spectrom , vol.20 , pp. 867-874
    • Jaskolla, T.W.1    Fuchs, B.2    Karas, M.3    Schiller, J.4
  • 22
    • 67650435354 scopus 로고    scopus 로고
    • BMSL UWO Biological Mass Spectrometry Laboratory home
    • BMSL UWO Biological Mass Spectrometry Laboratory homepage, http://www.biochem.uwo.ca/wits/bmsl/protocols.html.
  • 23
    • 67650385509 scopus 로고    scopus 로고
    • home
    • UniProt homepage, http://www.uniprot.org.
    • UniProt
  • 25
    • 0004214986 scopus 로고
    • Springer-Verlag: Berlin, Heidelberg, NewYork
    • Keil, B. Specificity of Proteolysis; Springer-Verlag: Berlin, Heidelberg, NewYork, 1992; p 335.
    • (1992) Specificity of Proteolysis , pp. 335
    • Keil, B.1
  • 27
    • 1242339573 scopus 로고    scopus 로고
    • Screening for N-glycosylated proteins by liquid chromatography mass spectrometry
    • Bunkenborg, J.; Pilch, B. J.; Podtelejnikov, A. V.; Wisniewski, J. R. Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics 2004, 4, 454-465.
    • (2004) Proteomics , vol.4 , pp. 454-465
    • Bunkenborg, J.1    Pilch, B.J.2    Podtelejnikov, A.V.3    Wisniewski, J.R.4
  • 28
    • 29144459934 scopus 로고    scopus 로고
    • Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry
    • Liu, T.; Qian, W.-J.; Gritsenko, M. A.; Camp, D. G. II.; Monroe, M. E.; Moore, R. J.; Smith, R. D. Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J. Proteome Res. 2005, 4, 2070-2080.
    • (2005) J. Proteome Res , vol.4 , pp. 2070-2080
    • Liu, T.1    Qian, W.-J.2    Gritsenko, M.A.3    Camp II, D.G.4    Monroe, M.E.5    Moore, R.J.6    Smith, R.D.7
  • 29
    • 33745000741 scopus 로고    scopus 로고
    • Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry
    • Ramachandran, P.; Boontheung, P.; Xie, Y.; Sondej, M.; Wong, D. T.; Loo, J. A. Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J. Proteome Res. 2006, 5, 1493-1503.
    • (2006) J. Proteome Res , vol.5 , pp. 1493-1503
    • Ramachandran, P.1    Boontheung, P.2    Xie, Y.3    Sondej, M.4    Wong, D.T.5    Loo, J.A.6
  • 30
    • 33947192955 scopus 로고    scopus 로고
    • Wada, Y.; Azadi, P.; Costello, C. E.; Dell, A.; Dwek, R. A.; Geyer, H.; Geyer, R.; Kakehi, K.; Karlsson, N. G.; Kato, K.; Kawasaki, N.; Khoo, K. H.; Kim, S.; Kondo, a.; Lattova, E.; Mechref, Y.; Miyoshi, E.; Nakamura, K.; Narimatsu, H.; Novotny, M. V.; Packer, N. H.; Perreault, H.; Peter-Katalinić, J.; Pohlentz, G.; Reinhold, V. N.; Rudd, P. M.; Suzuki, A.; Taniguchi, N. Comparison of the methods for profiling glycoprotein glycans - HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study. Glycobiology 2007, 17, 411-422.
    • Wada, Y.; Azadi, P.; Costello, C. E.; Dell, A.; Dwek, R. A.; Geyer, H.; Geyer, R.; Kakehi, K.; Karlsson, N. G.; Kato, K.; Kawasaki, N.; Khoo, K. H.; Kim, S.; Kondo, a.; Lattova, E.; Mechref, Y.; Miyoshi, E.; Nakamura, K.; Narimatsu, H.; Novotny, M. V.; Packer, N. H.; Perreault, H.; Peter-Katalinić, J.; Pohlentz, G.; Reinhold, V. N.; Rudd, P. M.; Suzuki, A.; Taniguchi, N. Comparison of the methods for profiling glycoprotein glycans - HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study. Glycobiology 2007, 17, 411-422.
  • 31
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N.; Pappin, D. J.; Creasy, D. M.; Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20, 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 33
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J.; Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157, 105-132.
    • (1982) J. Mol. Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.