Isotope-labeling strategy for the assignment of protein fragments generated for mass spectrometry

Journal of the American Chemical Society

Volumn 118, Issue 31, 1996, Pages 7402-7403

  Miranker, Andrew ^a   Kruppa, Gary H ^b   Robinson, Carol V ^a   Aplin, Robin T ^a   Dobson, Christopher M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b Bruker Instruments Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME;

ARTICLE; ISOTOPE LABELING; MASS SPECTROMETRY; PROTEIN ANALYSIS; TECHNIQUE;

EID: 0029769671     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9531236     Document Type: Article

References (30)

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15. 2O at pH 3.8 to remove residual salts. All FTMS spectra were recorded on a Bruker Bio-APEX 47e spectrometer equipped with a 4.7 T magnet, external ion source, and electrospray source (Analytica of Branford, Branford, CT). Ions were accumulated in the FTMS trap for 300 ms, followed by chirp excitation and detection with a 240 kHz bandwidth. Parent multiply charged molecular ions of lysozyme were observed with a capillary skimmer potential of 60-100 V, while for CID spectra the capillary skimmer potential was increased to 160-250 V. Calibration was performed against a mixture of peptides.
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