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Comparative peptide mapping of a hepatitis C viral recombinant protein by capillary electrophoresis and matrix-assisted laser desorption time-of-flight mass spectrometry

Capillary electrophoresis (CE) and matrix-assisted laser desorption time-of-flight mass spectrometry (MALDI-TOF-MS) were investigated as alternatives to sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis for peptide mapping with Staphylococcus aureus protease (V8) of a hydrophobic recom...

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Bibliographic Details
Published in:Journal of Chromatography A 1996-09, Vol.744 (1), p.177-185
Main Authors: Winkler, Martin A., Kundu, Samar, Robey, Thomas E., Gerard Robey, W.
Format: Article
Language:English
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Summary:Capillary electrophoresis (CE) and matrix-assisted laser desorption time-of-flight mass spectrometry (MALDI-TOF-MS) were investigated as alternatives to sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis for peptide mapping with Staphylococcus aureus protease (V8) of a hydrophobic recombinant hepatitis C virus antigen, HC-31, which required 0.1% SDS for solubility. Controls (V8 only) or HC-31 digests were extracted with chloroform-methanol-water (1:4:3) to remove SDS, which interferes with MALDI-TOF, and high salt content, which affects CE. In two different runs by CE, the elution times of each of 11 peptide peaks were very reproducible ( R. S. D.
ISSN:0021-9673
DOI:10.1016/0021-9673(96)00184-7