N-Terminal sequencing by mass spectrometry through specific fluorescamine labeling of α-amino groups before tryptic digestion

Analytical Biochemistry

Volumn 408, Issue 2, 2011, Pages 263-268

  Dhaunta, Neeraj ^a   Fatima, Uzma ^a   Guptasarma, Purnananda ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

Author keywords

Fluorescamine adduction; Mass spectrometry; N terminal sequencing; PH effects; Protein sequencing; Amino group reactivity

Indexed keywords

ALKALINITY; PH EFFECTS; PROTEINS;

ACIDIC CONDITIONS; ALKALINE CONDITIONS; AMINO GROUP; FLUORESCAMINES; N-TERMINAL SEQUENCING; N-TERMINALS; PROTEIN SEQUENCING; TRYPTIC DIGESTION;

MASS SPECTROMETRY;

ALPHA AMINO ACID; CRYSTALLIN; FLUORESCAMINE; LYSOZYME; TRYPSIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN DEGRADATION;

EID: 78149415742     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.09.013     Document Type: Article

References (17)

1. Weigele M., De Bernardo S.L., Tengi J.P., Leimgruber W. Novel reagent for the fluorometric assay of primary amines. J. Am. Chem. Soc. 1972, 94:5927-5928.
2. Udenfriend S., Stein S., Bohlen P., Dairman W., Leimgruber W., Weigele M. Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science 1972, 178:871-872.
3. Castell J.V., Cervera M., Marco R. A convenient micromethod for the assay of primary amines and proteins with fluorescamine: a re-examination of the conditions of reaction. Anal. Biochem. 1979, 99:379-391.
4. Bohlen P., Stein S., Udenfriend S. Studies on the reaction of fluorescamine with primary amines. Arch. Biochem. Biophys. 1974, 163:390-399.
5. Sampath-Kumar P.S., Fruton J. Studies on the extended active sites of acid proteinases. Proc. Natl Acad. Sci. USA 1974, 71:1070-1072.
6. Pritchard D.G., Schnute W.C., Todd C.W. Mass spectrometry of fluorescamine derivatives of amino acids and peptides. Biochem. Biophys. Res. Commun. 1975, 65:312-316.
7. Narasimhachari N. Mass spectra of the reaction products of some biologically important primary amines and fluorescamine. Biochem. Biophys. Res. Commun. 1973, 55:231-238.
8. Halim V.A., Muck A., Hartl M., Ibáñez A.J., Giri A., Erfurth F., Baldwin I.T., Svatos A. A dual fluorescent/MALDI chip platform for analyzing enzymatic activity and for protein profiling. Proteomics 2009, 9:171-181.
9. Nakai N., Lai C.Y., Horecker B.L. Use of fluorescamine in the chromatographic analysis of peptides from proteins. Anal. Biochem. 1974, 58:563-570.
10. Stein S., Bohlen P., Udenfriend S. Studies on the kinetics of reaction and hydrolysis of fluorescamine. Arch. Biochem. Biophys. 1974, 163:400-403.
11. Mendez E., Gavilanes J.G. Fluorometric detection of peptides after column chromatography or on paper: o-phthalaldehyde and fluorescamine. Anal. Biochem. 1976, 72:473-479.
12. Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat. Biotechnol. 2003, 21:566-569.
13. Van Damme P., Van Damme J., Demol H., Staes A., Vandekerckhove J., Gevaert K. A review of COFRADIC techniques targeting protein N-terminal acetylation. BMC Proc 2009, 3:S6.
14. Coussot G., Hawke D.H., Mularz A., Koomen J.M., Kobayashi R. A method for the isolation of blocked N-terminal peptides. Anal. Biochem. 2007, 361:302-304.
15. Mikami T., Takao T. Selective isolation of N-blocked peptides by isocyanate-coupled resin. Anal. Chem. 2007, 79:7910-7915.
16. Zhao L., Zhang Y., Wei J., Cao D., Liu K., Qian X. A rapid isolation and identification method for blocked N-terminal peptides by isothiocyanate-coupled magnetic nanoparticles and MS. Proteomics 2009, 9:4416-4420.
17. Kundu B., Shukla A., Guptasarma P. Peptide scanning-based identification of regions of γ-II crystallin involved in thermal aggregation: evidence of the involvement of structurally-analogous helix-containing loops from the two double Greek key domains of the molecule. Arch. Biochem. Biophys. 2003, 410:69-75.