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Volumn 68, Issue 1, 2007, Pages 115-127

Protein extraction from Mycobacterium avium subsp. paratuberculosis: Comparison of methods for analysis by sodium dodecyl sulphate polyacrylamide gel electrophoresis, native PAGE and surface enhanced laser desorption/ionization time of flight mass spectrometry

Author keywords

Lysis buffers; Native PAGE; Paratuberculosis; SDS PAGE; SELDI TOF MS

Indexed keywords

BACTERIAL PROTEIN; DETERGENT; POLYSORBATE 20; PROTEOME; SINAPIC ACID; THIOCYANATE POTASSIUM; TRITON X 100; UREA;

EID: 33845989503     PISSN: 01677012     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mimet.2006.07.003     Document Type: Article
Times cited : (13)

References (37)
  • 1
    • 6344284935 scopus 로고    scopus 로고
    • The use of proteomics for the assessment of clinical samples in research
    • Aldred S., Grant M.M., and Griffiths H.R. The use of proteomics for the assessment of clinical samples in research. Clin. Biochem. 37 (2004) 943-952
    • (2004) Clin. Biochem. , vol.37 , pp. 943-952
    • Aldred, S.1    Grant, M.M.2    Griffiths, H.R.3
  • 2
    • 9244231984 scopus 로고    scopus 로고
    • Application of the genome sequence to address concerns that Mycobacterium avium subspecies paratuberculosis might be a foodborne pathogen
    • Bannantine J.P., Barletta R.G., Stabel J.R., Paustian M.L., and Kapur V. Application of the genome sequence to address concerns that Mycobacterium avium subspecies paratuberculosis might be a foodborne pathogen. Foodborne Pathog. Dis. 1 (2004) 3-15
    • (2004) Foodborne Pathog. Dis. , vol.1 , pp. 3-15
    • Bannantine, J.P.1    Barletta, R.G.2    Stabel, J.R.3    Paustian, M.L.4    Kapur, V.5
  • 3
    • 0042088998 scopus 로고    scopus 로고
    • Gel electrophoresis under denaturating conditions
    • Wiley-Liss, New York
    • Bollag D.M., Edelstein S.J., and Rozycki M.D. Gel electrophoresis under denaturating conditions. Protein Methods (1996), Wiley-Liss, New York 107-154
    • (1996) Protein Methods , pp. 107-154
    • Bollag, D.M.1    Edelstein, S.J.2    Rozycki, M.D.3
  • 4
    • 0009642331 scopus 로고    scopus 로고
    • Gel electrophoresis under non-denaturating conditions
    • Wiley-Liss, New York
    • Bollag D.M., Edelstein S.J., and Rozycki M.D. Gel electrophoresis under non-denaturating conditions. Protein Methods (1996), Wiley-Liss, New York 155-172
    • (1996) Protein Methods , pp. 155-172
    • Bollag, D.M.1    Edelstein, S.J.2    Rozycki, M.D.3
  • 6
    • 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. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0029061399 scopus 로고
    • The envelope of mycobacteria
    • Brennan P.J. The envelope of mycobacteria. Ann. Rev. Biochem. 64 (1995) 29-63
    • (1995) Ann. Rev. Biochem. , vol.64 , pp. 29-63
    • Brennan, P.J.1
  • 8
    • 0037311923 scopus 로고    scopus 로고
    • Cordingley, H. C., Roberts, S. L., Tooke, P., Armitage, J. R., Lane, P. W., Wu, W., Wildsmith, S. E., 2003. Multifactorial screening design and analysis of SELDI-TOF ProteinChip array optimization experiments. Biotechniques. 34, 364-365, 368-373.
  • 10
    • 0001798501 scopus 로고    scopus 로고
    • Immunoprecipitation
    • Cold Spring Harbor Laboratory Press
    • Edward H. Immunoprecipitation. Using Antibodies: A Laboratory Manual (1999), Cold Spring Harbor Laboratory Press 230-231
    • (1999) Using Antibodies: A Laboratory Manual , pp. 230-231
    • Edward, H.1
  • 11
    • 0001232852 scopus 로고    scopus 로고
    • Non denaturating polyacrylamide gel electrophoresis
    • Oxford University Press, New York
    • Hames B.D. Non denaturating polyacrylamide gel electrophoresis. Gel Electrophoresis of Proteins: A Practical Approach (1998), Oxford University Press, New York 35-40
    • (1998) Gel Electrophoresis of Proteins: A Practical Approach , pp. 35-40
    • Hames, B.D.1
  • 12
    • 0014499213 scopus 로고
    • Solubilization of particulate proteins and nonelectrolytes by chaotropic agents
    • Hatefi Y., and Hanstein W.G. Solubilization of particulate proteins and nonelectrolytes by chaotropic agents. Proc. Natl. Acad. Sci. U. S. A. 62 (1969) 1129-1136
    • (1969) Proc. Natl. Acad. Sci. U. S. A. , vol.62 , pp. 1129-1136
    • Hatefi, Y.1    Hanstein, W.G.2
  • 13
    • 84990629710 scopus 로고
    • New desorption strategies for the mass spectrometric analysis of macromolecules
    • Hutchens T.W., and Yip T.T. New desorption strategies for the mass spectrometric analysis of macromolecules. Rapid Commun. Mass Spectrom. 7 (1993) 576-580
    • (1993) Rapid Commun. Mass Spectrom. , vol.7 , pp. 576-580
    • Hutchens, T.W.1    Yip, T.T.2
  • 14
    • 0036079692 scopus 로고    scopus 로고
    • The SELDI-TOF MS approach to proteomics: protein profiling and biomarker identification
    • Issaq H.J., Veenstra T.D., Conrads T.P., and Felschow D. The SELDI-TOF MS approach to proteomics: protein profiling and biomarker identification. Biochem. Biophys. Res. Commun. 292 (2002) 587-592
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 587-592
    • Issaq, H.J.1    Veenstra, T.D.2    Conrads, T.P.3    Felschow, D.4
  • 15
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 Da
    • Karas M., and Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 Da. Anal. Chem. 60 (1988) 2299-2301
    • (1988) Anal. Chem. , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0041530024 scopus 로고    scopus 로고
    • Mutational analysis of cell wall biosynthesis in Mycobacterium avium
    • Laurent J.P., Hauge K., Burnside K., and Cangelosi G. Mutational analysis of cell wall biosynthesis in Mycobacterium avium. J. Bacteriol. 185 (2003) 5003-5006
    • (2003) J. Bacteriol. , vol.185 , pp. 5003-5006
    • Laurent, J.P.1    Hauge, K.2    Burnside, K.3    Cangelosi, G.4
  • 21
    • 33644863647 scopus 로고    scopus 로고
    • Genomic comparison of Mycobacterium avium subsp. paratuberculosis sheep and cattle strains by microarray hybridization
    • Marsh I.B., Bannantine J.P., Paustian M.L., Tizard M., Kapur V., and Whittington R.J. Genomic comparison of Mycobacterium avium subsp. paratuberculosis sheep and cattle strains by microarray hybridization. J. Bacteriol. 188 (2006) 2290-2293
    • (2006) J. Bacteriol. , vol.188 , pp. 2290-2293
    • Marsh, I.B.1    Bannantine, J.P.2    Paustian, M.L.3    Tizard, M.4    Kapur, V.5    Whittington, R.J.6
  • 22
    • 0034013944 scopus 로고    scopus 로고
    • Recent advancements in surface-enhanced laser desorption/ionization-time of flight-mass spectrometry
    • Merchant M., and Weinberger S.R. Recent advancements in surface-enhanced laser desorption/ionization-time of flight-mass spectrometry. Electrophoresis 21 (2000) 1164-1177
    • (2000) Electrophoresis , vol.21 , pp. 1164-1177
    • Merchant, M.1    Weinberger, S.R.2
  • 23
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff V., Arold N., Taube D., and Ehrhardt W. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9 (1988) 255-262
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 24
    • 0040162268 scopus 로고    scopus 로고
    • The mycobacteria: an introduction to nomenclature and pathogenesis
    • Rastogi N., Legrand E., and Sola C. The mycobacteria: an introduction to nomenclature and pathogenesis. Rev. Sci. Tech. 20 (2001) 21-54
    • (2001) Rev. Sci. Tech. , vol.20 , pp. 21-54
    • Rastogi, N.1    Legrand, E.2    Sola, C.3
  • 25
    • 27544449360 scopus 로고    scopus 로고
    • Effective interactions between chaotropic agents and proteins
    • Salvi G., De Los Rios P., and Vendruscolo M. Effective interactions between chaotropic agents and proteins. Proteins 61 (2005) 492-499
    • (2005) Proteins , vol.61 , pp. 492-499
    • Salvi, G.1    De Los Rios, P.2    Vendruscolo, M.3
  • 26
    • 0346101481 scopus 로고    scopus 로고
    • Urine protein profiling with surface-enhanced laser-desorption/ionization time-of-flight mass spectrometry
    • Schaub S., Wilkins J., Weiler T., Sangster K., Rush D., and Nickerson P. Urine protein profiling with surface-enhanced laser-desorption/ionization time-of-flight mass spectrometry. Kidney Int. 65 (2004) 323-332
    • (2004) Kidney Int. , vol.65 , pp. 323-332
    • Schaub, S.1    Wilkins, J.2    Weiler, T.3    Sangster, K.4    Rush, D.5    Nickerson, P.6
  • 27
    • 3242701625 scopus 로고    scopus 로고
    • Surface-enhanced laser desorption ionization time-of-flight mass spectrometry (SELDI TOF-MS) and ProteinChip technology in proteomics research
    • Seibert V., Wiesner A., Buschmann T., and Meuer J. Surface-enhanced laser desorption ionization time-of-flight mass spectrometry (SELDI TOF-MS) and ProteinChip technology in proteomics research. Pathol. Res. Pract. 200 (2004) 83-94
    • (2004) Pathol. Res. Pract. , vol.200 , pp. 83-94
    • Seibert, V.1    Wiesner, A.2    Buschmann, T.3    Meuer, J.4
  • 29
    • 84874104894 scopus 로고    scopus 로고
    • Nondenaturating PAGE of proteins
    • Cold Spring Harbor Laboratory Press, New York
    • Simpson R.J. Nondenaturating PAGE of proteins. Proteins and Proteomics (2003), Cold Spring Harbor Laboratory Press, New York 85-86
    • (2003) Proteins and Proteomics , pp. 85-86
    • Simpson, R.J.1
  • 30
    • 1642405376 scopus 로고    scopus 로고
    • Possible association of GroES and antigen 85 proteins with heat resistance of Mycobacterium paratuberculosis
    • Sung N., Takayama K., and Collins M.T. Possible association of GroES and antigen 85 proteins with heat resistance of Mycobacterium paratuberculosis. Appl. Environ. Microbiol. 70 (2004) 1688-1697
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 1688-1697
    • Sung, N.1    Takayama, K.2    Collins, M.T.3
  • 31
    • 0036020660 scopus 로고    scopus 로고
    • Protein microarrays: challenges and promises
    • Talapatra A., Rouse R., and Hardiman G. Protein microarrays: challenges and promises. Pharmacogenomics 3 (2002) 527-536
    • (2002) Pharmacogenomics , vol.3 , pp. 527-536
    • Talapatra, A.1    Rouse, R.2    Hardiman, G.3
  • 32
    • 0028528740 scopus 로고
    • Comparison of cellular and extracellular proteins expressed by various isolates of Mycobacterium paratuberculosis and other mycobacterial species
    • White W.B., Whipple D.L., Stabel J.R., and Bolin C.A. Comparison of cellular and extracellular proteins expressed by various isolates of Mycobacterium paratuberculosis and other mycobacterial species. Am. J. Vet. Res. 55 (1994) 1399-1405
    • (1994) Am. J. Vet. Res. , vol.55 , pp. 1399-1405
    • White, W.B.1    Whipple, D.L.2    Stabel, J.R.3    Bolin, C.A.4
  • 33
    • 3042541639 scopus 로고    scopus 로고
    • Bioinformatics strategies for proteomic profiling
    • White C.N., Chan D.W., and Zhang Z. Bioinformatics strategies for proteomic profiling. Clin. Biochem. 37 (2004) 636-641
    • (2004) Clin. Biochem. , vol.37 , pp. 636-641
    • White, C.N.1    Chan, D.W.2    Zhang, Z.3
  • 34
    • 0031938859 scopus 로고    scopus 로고
    • Rapid detection of Mycobacterium paratuberculosis in clinical samples from ruminants and in spiked environmental samples by modified BACTEC 12B radiometric culture and direct confirmation by IS900 PCR
    • Whittington R.J., Marsh I., Turner M.J., McAllister S., Choy E., Eamens G.J., Marshall D.J., and Ottaway S. Rapid detection of Mycobacterium paratuberculosis in clinical samples from ruminants and in spiked environmental samples by modified BACTEC 12B radiometric culture and direct confirmation by IS900 PCR. J. Clin. Microbiol. 36 (1998) 701-707
    • (1998) J. Clin. Microbiol. , vol.36 , pp. 701-707
    • Whittington, R.J.1    Marsh, I.2    Turner, M.J.3    McAllister, S.4    Choy, E.5    Eamens, G.J.6    Marshall, D.J.7    Ottaway, S.8
  • 35
    • 0033041245 scopus 로고    scopus 로고
    • Evaluation of modified BACTEC 12B radiometric medium and solid media for culture of Mycobacterium avium subsp. paratuberculosis from sheep
    • Whittington R.J., Marsh I., McAllister S., Turner M.J., Marshall D.J., and Fraser C.A. Evaluation of modified BACTEC 12B radiometric medium and solid media for culture of Mycobacterium avium subsp. paratuberculosis from sheep. J. Clin. Microbiol. 37 (1999) 1077-1083
    • (1999) J. Clin. Microbiol. , vol.37 , pp. 1077-1083
    • Whittington, R.J.1    Marsh, I.2    McAllister, S.3    Turner, M.J.4    Marshall, D.J.5    Fraser, C.A.6
  • 36
    • 0033632255 scopus 로고    scopus 로고
    • Temporal patterns and quantification of excretion of Mycobacterium avium subsp. paratuberculosis in sheep with Johne's disease
    • Whittington R.J., Reddacliff L.A., Marsh I., McAllister S., and Saunders V. Temporal patterns and quantification of excretion of Mycobacterium avium subsp. paratuberculosis in sheep with Johne's disease. Aust. Vet. J. 78 (2000) 34-37
    • (2000) Aust. Vet. J. , vol.78 , pp. 34-37
    • Whittington, R.J.1    Reddacliff, L.A.2    Marsh, I.3    McAllister, S.4    Saunders, V.5


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