Analysis of Proteins by Direct-Scanning Infrared-MALDI Mass Spectrometry after 2D-PAGE Separation and Electroblotting

Analytical Chemistry

Volumn 69, Issue 15, 1997, Pages 2888-2892

  Eckerskorn, Christoph ^a,b   Strupat, Kerstin ^a,b   Schleuder, Detlev ^a   Hochstrasser, Denis ^c   Sanchez, Jean Charles ^c   Lottspeich, Friedrich ^b   Hillenkamp, Franz ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^c GENEVA UNIVERSITY HOSPITALS   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

PLASMA PROTEIN;

ARTICLE; HUMAN; INFRARED SPECTROPHOTOMETRY; MASS SPECTROMETRY; METHODOLOGY; TWO DIMENSIONAL GEL ELECTROPHORESIS; WESTERN BLOTTING;

BLOOD PROTEINS; BLOTTING, WESTERN; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; HUMANS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SPECTROPHOTOMETRY, INFRARED;

EID: 0031202984     PISSN: 00032700     EISSN: None     Source Type: Journal    
DOI: 10.1021/ac970077e     Document Type: Article

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35. To confirm the masses, the haptoglobin α2 proteins were eluted from the gel and analyzed by LC/ESI-MS. The obtained masses for the pyridylethylated forms were (16 682.1 ± 3), (16 683.0 ± 2), and (16 839.0 ± 3) Da, for proteins A, B, and C, respectively. The difference between spots B and C of 156.0 Da (ESI-MS data) corresponds to the C-terminal Arg of the processing side.
36. Schleuder, D.; Strupat, K.; Eckerskorn, C.; Hillenkamp, F. Manuscript in preparation.