Identification of proteins in cell-free extracts using liquid chromatography-electrospray ionization mass spectrometry

BioTechniques

Volumn 28, Issue 1, 2000, Pages 156-160

  Dalluge, Joseph J ^a   Reddy, Prasad ^a  

^a NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PHOSPHOENOLPYRUVATE;

ANALYTIC METHOD; ARTICLE; ESCHERICHIA COLI; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NONHUMAN; PLASMID; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0033989216     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/00281rr04     Document Type: Article

References (18)

1. Beavis, R.C. and B.T. Chait. 1990. Rapid, sensitive analysis of protein mixtures by mass spectrometry. Proc. Natl. Acad. Sci. USA 87:6873-6877.
2. Cain, T.C., D.M. Lubman and W.J. Weber, Jr. 1994. Differentiation of bacteria using protein profiles from matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 8:1026-1030.
3. Chong, B.E., D.B. Wall, D.M. Lubman and S.J. Flynn. 1997. Rapid profiling of E. coli proteins up to 500 kDa from whole cell lystates using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 11:1900-1908.
4. Dorschug, M., R. Frank, H. R. Kalbitzer, W. Hengstenberg and J. Deutscher. 1984. Phosphoenolpyruvate-dependent phosphorylation site in enzyme IIIglc of the Escherichia coli phosphotransferase system. Eur. J. Biochem. 144:113-119.
5. Easterling, M.L., C.M. Colangelo, R.A. Scott and I.J. Amster. 1998. Monitoring protein expression in whole bacteria cells with MALDI time-of-flight mass spectrometry. Anal. Chem. 70:2704-2709.
6. Fenn, J.B., M. Mann, C.K. Meng, S.F. Wong and C.M. Whitehouse. 1989. Electrospray ionization for mass spectrometry of large biomolecules. Science 246:64-71.
7. Gersten, D.M. 1996. Gel Electrophoresis:Proteins. John Wiley and Sons, New York, NY.
8. Goeddel, D.V. 1990. Methods Enzymol: Vol. 185, Gene Expression Technology. Academic Press, New York, NY.
9. Hung, K.C., H. Ding and B. Guo. 1999. Use of poly(tetrafluoroethylene)s as a sample support for the MALDI-TOF analysis of DNA and proteins. Anal. Chem. 71:518-521.
10. Karas, M., U. Bahr and F. Hillenkamp. 1989. UV laser matrix desorption ionization mass spectrometry of proteins in the 100 000 dalton range. Int. J. Mass Spectrom. Ion Processes 92:231-242.
11. Karas, M. and F. Hillenkamp. 1988. Laser desorption ionization of proteins with molecular masses exceeding 10 000 daltons. Anal. Chem. 60:2301-2303.
12. Lowry, O.H., N.J. Rosebrough, A.L. Farr and R.J. Randall. 1951. Protein measurement with Folin phenol reagent. J. Biol. Chem. 193:265-275.
13. Rao, R.N. 1984. Construction and properties of plasmid pKC30, a pBR322 derivative containing the PL-N region of phage lambda. Gene 31:247-250.
14. Reddy, P., N. Fredd-Kuldell, E. Liberman and A. Peterkofsky. 1991. Overproduction and rapid purification of the phosphoenolpyruvate:sugar phosphotransferase system proteins Enzyme I, HPr and Protein IIIGlc of Escherichia coli. Protein Exp. Purif. 2:179-187.
15. Reddy, P., A. Peterkofsky and K. McKenney. 1989. Hyperexpression and purification of Escherichia coli adenylate cyclase using a vector designed for expression of lethal gene products. Nucleic Acids Res. 17:10473-10488.
16. Saffen, D.W., K.A. Presper, T.L. Doering and S. Roseman. 1987. Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI and crr genes. J. Biol. Chem. 262:16241-16253.
17. Worrall, T.A., R.J. Cotter and A.S. Woods. 1998. Purification of contaminated peptides and proteins on synthetic membrane surfaces for matrix-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 70:750-756.
18. Zuber, M., T.A. Patterson and D.L. Court 1987. Analysis of nutR, a site required for transcription antitermination in phage lambda. Proc. Natl. Acad. Sci. USA. 84:4514-4518.