Detection of M-Protein in Acetonitrile Precipitates of Serum using MALDI-TOF Mass Spectrometry
N. Mehra, G. Gopisetty, J. Subramani, A. Rajamanickam, S. Sundersingh, P. Karunakaran, J. Perumal Kalaiyarasi, K. Kannan, V. Radhakrishnan, S. Tenali Gnana, R. Thangarajan
Abstract
Purpose of the researchMultiple myeloma and plasmacytomas belong to a group of disorders, namely plasma cell dyscrasias and are identified by the presence of a monoclonal protein (M-protein). MALDI-TOF-mass spectrometry (MS) has demonstrated superior analytical sensitivity for the detection of M-protein and is now used for screening of M-protein at some centres. We present the results of an alternative methodology for M-protein analysis by MALDI-TOF MS. MethodsSerum samples from patients with newly diagnosed multiple myeloma or plasmacytoma with positive M-protein detected by serum protein electrophoresis, immunofixation electrophoresis and serum free light chain analysis, underwent direct reagent-based extraction process using Acetonitrile (ACN) precipitation. Serum{kappa} and{lambda} light chains were validated using immunoenrichment by anti-{kappa} and anti-{lambda} biotin-labelled antibodies immobilised on streptavidin magnetic beads. MALDI-TOF MS measurements were obtained for intact proteins using alpha-cyano-4-hydroxycinnamic acid as matrix. The images obtained were overlaid on apparently healthy donor serum samples to confirm the presence of M-protein. Principle resultsCharacteristic M-protein peaks were observed in the ACN precipitates of serum in the predicted mass ranges for{kappa} and{lambda} . The{kappa} and{lambda} peaks were confirmed by immunoenrichment analysis. Twenty-seven patient samples with either newly diagnosed multiple myeloma or plasmacytoma with monoclonal gammopathy detected by the standard methods were chosen for Acetonitrile precipitation and analysed by MALDI-TOF MS. All 27 patient samples demonstrated a peak suggestive of M-protein with mass/charge (m/z) falling within the{kappa} and{lambda} range. The concordance rate with serum immunofixation electrophoresis and free light chain analysis was above 90%. Major conclusionsWe report the results of a low-cost reagent-based extraction process using Acetonitrile precipitation to enrich for{kappa} and{lambda} light chains, which can be used for the screening and qualitative analysis of M-protein.
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