메뉴 건너뛰기




Volumn 1834, Issue 6, 2013, Pages 1222-1229

Accessing the reproducibility and specificity of pepsin and other aspartic proteases

Author keywords

Aspergillopepsin; Factor XIII; Hydrogen exchange; Mass spectrometry; Online digestion; Rice field eel

Indexed keywords

ARGININE; ASPARAGINE; ASPARTIC PROTEINASE; ASPERGILLOPEPSIN; GLYCINE; PEPSIN A; UNCLASSIFIED DRUG;

EID: 84878108052     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.10.003     Document Type: Article
Times cited : (122)

References (40)
  • 1
    • 0028009220 scopus 로고
    • High-accuracy mass measurement as a tool for studying proteins
    • R. Wang, and B.T. Chait High-accuracy mass measurement as a tool for studying proteins Curr. Opin. Biotechnol. 5 1994 77 84
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 77-84
    • Wang, R.1    Chait, B.T.2
  • 4
    • 0015217218 scopus 로고
    • Fluorescent probes for conformational states of proteins. IV. The pepsinogen-pepsin conversion
    • J.L. Wang, and G.M. Edelman Fluorescent probes for conformational states of proteins. IV. The pepsinogen-pepsin conversion J. Biol. Chem. 246 1971 1185 1191
    • (1971) J. Biol. Chem. , vol.246 , pp. 1185-1191
    • Wang, J.L.1    Edelman, G.M.2
  • 5
    • 58149144529 scopus 로고    scopus 로고
    • Synchrotron small-angle X-ray scattering studies of the structure of porcine pepsin under various pH conditions
    • K.S. Jin, Y. Rho, J. Kim, H. Kim, I.J. Kim, and M. Ree Synchrotron small-angle X-ray scattering studies of the structure of porcine pepsin under various pH conditions J. Phys. Chem. B 112 2008 15821 15827
    • (2008) J. Phys. Chem. B , vol.112 , pp. 15821-15827
    • Jin, K.S.1    Rho, Y.2    Kim, J.3    Kim, H.4    Kim, I.J.5    Ree, M.6
  • 6
    • 73049084464 scopus 로고    scopus 로고
    • Recombinant prosegment peptide acts as a folding catalyst and inhibitor of native pepsin
    • D.R. Dee, S. Filonowicz, Y. Horimoto, and R.Y. Yada Recombinant prosegment peptide acts as a folding catalyst and inhibitor of native pepsin Biochim. Biophys. Acta 1794 2009 1795 1801
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1795-1801
    • Dee, D.R.1    Filonowicz, S.2    Horimoto, Y.3    Yada, R.Y.4
  • 7
    • 0035987666 scopus 로고    scopus 로고
    • A history of pepsin and related enzymes
    • J.S. Fruton A history of pepsin and related enzymes Q. Rev. Biol. 77 2002 127 147
    • (2002) Q. Rev. Biol. , vol.77 , pp. 127-147
    • Fruton, J.S.1
  • 8
  • 10
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Z. Zhang, and D.L. Smith Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation Protein Sci. 2 1993 522 531
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 11
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • T.E. Wales, and J.R. Engen Hydrogen exchange mass spectrometry for the analysis of protein dynamics Mass Spectrom. Rev. 25 2006 158 170
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 12
    • 0018801332 scopus 로고
    • An experimental procedure for increasing the structural resolution of chemical hydrogen-exchange measurements on proteins: Application to ribonuclease S peptide
    • J.J. Rosa, and F.M. Richards An experimental procedure for increasing the structural resolution of chemical hydrogen-exchange measurements on proteins: Application to ribonuclease S peptide J. Mol. Biol. 133 1979 399 416
    • (1979) J. Mol. Biol. , vol.133 , pp. 399-416
    • Rosa, J.J.1    Richards, F.M.2
  • 13
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • S.W. Englander, and N.R. Kallenbach Hydrogen exchange and structural dynamics of proteins and nucleic acids Q. Rev. Biophys. 16 1983 521 655
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 14
    • 0022426014 scopus 로고
    • Protein hydrogen exchange studied by the fragment separation method
    • J.J. Englander, J.R. Rogero, and S.W. Englander Protein hydrogen exchange studied by the fragment separation method Anal. Biochem. 147 1985 234 244
    • (1985) Anal. Biochem. , vol.147 , pp. 234-244
    • Englander, J.J.1    Rogero, J.R.2    Englander, S.W.3
  • 15
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Z. Zhang, and D.L. Smith Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation Protein Sci. 2 1993 522 531
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 16
    • 0033557450 scopus 로고    scopus 로고
    • Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/protein interactions
    • H. Ehring Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/protein interactions Anal. Biochem. 267 1999 252 259
    • (1999) Anal. Biochem. , vol.267 , pp. 252-259
    • Ehring, H.1
  • 17
    • 0036463721 scopus 로고    scopus 로고
    • Hydrogen exchange-mass spectrometry: Optimization of digestion conditions
    • L. Wang, H. Pan, and D.L. Smith Hydrogen exchange-mass spectrometry: Optimization of digestion conditions Mol. Cell Proteomics 1 2002 132 138
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 132-138
    • Wang, L.1    Pan, H.2    Smith, D.L.3
  • 18
    • 0014940725 scopus 로고
    • Secondary enzyme-substrate interactions and the specificity of pepsin
    • G.P. Sachdev, and J.S. Fruton Secondary enzyme-substrate interactions and the specificity of pepsin Biochemistry 9 1970 4465 4470
    • (1970) Biochemistry , vol.9 , pp. 4465-4470
    • Sachdev, G.P.1    Fruton, J.S.2
  • 19
  • 22
  • 24
    • 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
    • L. Cravello, D. Lascoux, and E. Forest 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. 17 2003 2387 2393
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 2387-2393
    • Cravello, L.1    Lascoux, D.2    Forest, E.3
  • 26
    • 84878956229 scopus 로고    scopus 로고
    • Hydrogen Exchange Mass Spectrometry for Conformational Analysis of Proteins
    • R.A. Meyers, Wiley 10.1002/9780470027318.a9780470029201
    • J.R. Engen, T.E. Wales, and X. Shi Hydrogen Exchange Mass Spectrometry for Conformational Analysis of Proteins R.A. Meyers, Encyclopedia of Analytical Chemistry 2011 Wiley 10.1002/9780470027318.a9780470029201
    • (2011) Encyclopedia of Analytical Chemistry
    • Engen, J.R.1    Wales, T.E.2    Shi, X.3
  • 27
    • 33947599164 scopus 로고    scopus 로고
    • Defining the interacting regions between apomyoglobin and lipid membrane by hydrogen/deuterium exchange coupled to mass spectrometry
    • P. Man, C. Montagner, G. Vernier, B. Dublet, A. Chenal, E. Forest, and V. Forge Defining the interacting regions between apomyoglobin and lipid membrane by hydrogen/deuterium exchange coupled to mass spectrometry J. Mol. Biol. 368 2007 464 472
    • (2007) J. Mol. Biol. , vol.368 , pp. 464-472
    • Man, P.1    Montagner, C.2    Vernier, G.3    Dublet, B.4    Chenal, A.5    Forest, E.6    Forge, V.7
  • 28
    • 57449107282 scopus 로고    scopus 로고
    • Enhanced digestion efficiency, peptide ionization efficiency, and sequence resolution for protein hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry
    • H.M. Zhang, S. Kazazic, T.M. Schaub, J.D. Tipton, M.R. Emmett, and A.G. Marshall Enhanced digestion efficiency, peptide ionization efficiency, and sequence resolution for protein hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry Anal. Chem. 80 2008 9034 9041
    • (2008) Anal. Chem. , vol.80 , pp. 9034-9041
    • Zhang, H.M.1    Kazazic, S.2    Schaub, T.M.3    Tipton, J.D.4    Emmett, M.R.5    Marshall, A.G.6
  • 29
    • 70449358536 scopus 로고    scopus 로고
    • Recombinant immobilized rhizopuspepsin as a new tool for protein digestion in hydrogen/deuterium exchange mass spectrometry
    • M. Rey, P. Man, G. Brandolin, E. Forest, and L. Pelosi Recombinant immobilized rhizopuspepsin as a new tool for protein digestion in hydrogen/deuterium exchange mass spectrometry Rapid Commun. Mass Spectrom. 23 2009 3431 3438
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 3431-3438
    • Rey, M.1    Man, P.2    Brandolin, G.3    Forest, E.4    Pelosi, L.5
  • 30
    • 73449142451 scopus 로고    scopus 로고
    • Investigating alternative acidic proteases for H/D exchange coupled to mass spectrometry: Plasmepsin 2 but not plasmepsin 4 is active under quenching conditions
    • J. Marcoux, E. Thierry, C. Vives, L. Signor, F. Fieschi, and E. Forest Investigating alternative acidic proteases for H/D exchange coupled to mass spectrometry: Plasmepsin 2 but not plasmepsin 4 is active under quenching conditions J. Am. Soc. Mass Spectrom. 21 2010 76 79
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 76-79
    • Marcoux, J.1    Thierry, E.2    Vives, C.3    Signor, L.4    Fieschi, F.5    Forest, E.6
  • 31
    • 85047690480 scopus 로고
    • Tuna pepsinogens and pepsins. Purification, characterization and amino-terminal sequences
    • M. Tanji, T. Kageyama, and K. Takahashi Tuna pepsinogens and pepsins. Purification, characterization and amino-terminal sequences Eur. J. Biochem. 177 1988 251 259
    • (1988) Eur. J. Biochem. , vol.177 , pp. 251-259
    • Tanji, M.1    Kageyama, T.2    Takahashi, K.3
  • 32
    • 0031679859 scopus 로고    scopus 로고
    • Purification and characterization of the main pepsinogen from the shark, Centroscymnus coelolepis
    • A.D. Nguyen, J. Nungaray, A. Martel, F. Le Goffic, D. Molle, and J. Leonil Purification and characterization of the main pepsinogen from the shark, Centroscymnus coelolepis J. Biochem. 124 1998 287 293
    • (1998) J. Biochem. , vol.124 , pp. 287-293
    • Nguyen, A.D.1    Nungaray, J.2    Martel, A.3    Le Goffic, F.4    Molle, D.5    Leonil, J.6
  • 34
    • 79960994826 scopus 로고    scopus 로고
    • Purification and characterization of pepsinogens and pepsins from the stomach of rice field eel (Monopterus albus Zuiew)
    • W.Y. Weng, T. Wu, W.Q. Chen, G.M. Liu, K. Osatomi, W.J. Su, and M.J. Cao Purification and characterization of pepsinogens and pepsins from the stomach of rice field eel (Monopterus albus Zuiew) Fish Physiol. Biochem. 37 2011 543 552
    • (2011) Fish Physiol. Biochem. , vol.37 , pp. 543-552
    • Weng, W.Y.1    Wu, T.2    Chen, W.Q.3    Liu, G.M.4    Osatomi, K.5    Su, W.J.6    Cao, M.J.7
  • 35
    • 51549121010 scopus 로고    scopus 로고
    • High-speed and high-resolution UPLC separation at zero degrees Celsius
    • T.E. Wales, K.E. Fadgen, G.C. Gerhardt, and J.R. Engen High-speed and high-resolution UPLC separation at zero degrees Celsius Anal. Chem. 80 2008 6815 6820
    • (2008) Anal. Chem. , vol.80 , pp. 6815-6820
    • Wales, T.E.1    Fadgen, K.E.2    Gerhardt, G.C.3    Engen, J.R.4
  • 37
    • 79954629044 scopus 로고    scopus 로고
    • MSTools-Web based application for visualization and presentation of HXMS data
    • D. Kavan, and P. Man MSTools-Web based application for visualization and presentation of HXMS data Int. J. Mass Spectrom. 302 2011 53 58
    • (2011) Int. J. Mass Spectrom. , vol.302 , pp. 53-58
    • Kavan, D.1    Man, P.2
  • 38
    • 33750617803 scopus 로고    scopus 로고
    • Improving digestion efficiency under H/D exchange conditions with activated pepsinogen coupled columns
    • S.A. Busby, M.J. Chalmers, and P.R. Griffin Improving digestion efficiency under H/D exchange conditions with activated pepsinogen coupled columns Int. J. Mass Spectrom. 259 2006 130 139
    • (2006) Int. J. Mass Spectrom. , vol.259 , pp. 130-139
    • Busby, S.A.1    Chalmers, M.J.2    Griffin, P.R.3
  • 39
    • 76849116408 scopus 로고    scopus 로고
    • Simultaneous reduction and digestion of proteins with disulfide bonds for hydrogen/deuterium exchange monitored by mass spectrometry
    • H.M. Zhang, S.M. McLoughlin, S.D. Frausto, H. Tang, M.R. Emmett, and A.G. Marshall Simultaneous reduction and digestion of proteins with disulfide bonds for hydrogen/deuterium exchange monitored by mass spectrometry Anal. Chem. 82 2010 1450 1454
    • (2010) Anal. Chem. , vol.82 , pp. 1450-1454
    • Zhang, H.M.1    Mcloughlin, S.M.2    Frausto, S.D.3    Tang, H.4    Emmett, M.R.5    Marshall, A.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.