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

David R. Barnidge, Thomas P. Krick, Timothy J Griffin, David L. Murray

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Rationale Use 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). Methods Samples were enriched for immunoglobulins in 5 min using Melon Gel™ followed by reduction with dithiothreitol for 15 min 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. Results Monoclonal immunoglobulin light chains were identified in serum and urine samples from patients with a known monoclonal gammopathy using MALDI-TOFMS with minimal sample preparation. Conclusions MALDI-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.

Original languageEnglish (US)
Pages (from-to)2057-2060
Number of pages4
JournalRapid Communications in Mass Spectrometry
Volume29
Issue number21
DOIs
StatePublished - Nov 15 2015

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Immunoglobulin Light Chains
Ionization
Mass spectrometry
Desorption
Electrophoresis
Gels
Immunoglobulins
Lasers
Proteins
Dithiothreitol
Molecular mass
Mass spectrometers

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Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry to detect monoclonal immunoglobulin light chains in serum and urine. / Barnidge, David R.; Krick, Thomas P.; Griffin, Timothy J; Murray, David L.

In: Rapid Communications in Mass Spectrometry, Vol. 29, No. 21, 15.11.2015, p. 2057-2060.

Research output: Contribution to journalArticle

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