4.4 Article

Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry to detect monoclonal immunoglobulin light chains in serum and urine

Journal

RAPID COMMUNICATIONS IN MASS SPECTROMETRY
Volume 29, Issue 21, Pages 2057-2060

Publisher

WILEY-BLACKWELL
DOI: 10.1002/rcm.7314

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RationaleUse of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) to monitor serum and urine samples for endogenous monoclonal immunoglobulins. MALDI-TOFMS is faster, fully automatable, and provides superior specificity compared to protein gel electrophoresis (PEL). MethodsSamples were enriched for immunoglobulins in 5min using Melon Gel followed by reduction with dithiothreitol for 15min to separate immunoglobulin light chains and heavy chains. Samples were then desalted using C4 ZipTips, mixed with sinapinic acid matrix, and analyzed on a Bruker Biflex III MALDI-TOF mass spectrometer. ResultsMonoclonal immunoglobulin light chains were identified in serum and urine samples from patients with a known monoclonal gammopathy using MALDI-TOFMS with minimal sample preparation. ConclusionsMALDI-TOFMS can identify a monoclonal immunoglobulin in serum and urine samples. The molecular mass of the monoclonal immunoglobulin light chain is obtained providing unprecedented specificity compared to PEL. In addition, the methodology can be automated, making it a practical alternative to PEL. Copyright (c) 2015 John Wiley & Sons, Ltd.

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