BIA/MS: Interfacing Biomolecular Interaction Analysis with Mass Spectrometry

Biomolecular interaction analysis (BIA) which utilizes surface plasmon resonance (SPR) detection of affinity-captured analytes has been interfaced with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI). Femtomole quantities of a peptide, myotoxina,were detected by...

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Bibliographic Details
Published in:Analytical biochemistry 1997-01, Vol.244 (1), p.124-132
Main Authors: Krone, Jennifer R., Nelson, Randall W., Dogruel, David, Williams, Peter, Granzow, Russ
Format: Article
Language:English
Subjects:
Biosensing Techniques
Crotalid Venoms - analysis
Sensitivity and Specificity
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
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Summary:Biomolecular interaction analysis (BIA) which utilizes surface plasmon resonance (SPR) detection of affinity-captured analytes has been interfaced with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI). Femtomole quantities of a peptide, myotoxina,were detected by direct MALDI analysis of sensor chips used during BIA of a polyclonal anti-myotoxinaIgG/myotoxinasystem. Further, different interactive surfaces (flow cells) present on a single biosensor were targeted individually for mass spectrometric analysis. System compatibility of the combined approach was demonstrated with sensitivities, detection limits, and analytical performances comparable to those intrinsic to the individual analyses. The combined approach unites the real-time capabilities of SPR-based BIA with the qualitative specificity of mass spectrometry.
ISSN:0003-2697
1096-0309
DOI:10.1006/abio.1996.9871