{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T22:03:26Z","timestamp":1790633006460,"version":"4.1.0"},"reference-count":52,"publisher":"Walter de Gruyter GmbH","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2016,1,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Serum immunoglobulin free light chains (FLC) are secreted into circulation by plasma cells as a by-product of immunoglobulin production. In a healthy individual the population of FLC is polyclonal as no single cell is secreting more FLC than the total immunoglobulin secreting cell population. In a person with a plasma cell dyscrasia, such as multiple myeloma (MM) or light chain amyloidosis (AL), a clonal population of plasma cells secretes a monoclonal light chain at a concentration above the normal polyclonal background.<\/jats:p>\n                  <jats:p>We recently showed that monoclonal immunoglobulin rapid accurate mass measurement (miRAMM) can be used to identify and quantify a monoclonal light chain (LC) in serum and urine above the polyclonal background. This was accomplished by reducing immunoglobulin disulfide bonds releasing the LC to be analyzed by microLC-ESI-Q-TOF mass spectrometry. Here we demonstrate that the methodology can also be applied to the detection and quantification of FLC by analyzing a non-reduced sample.<\/jats:p>\n                  <jats:p>Proof of concept experiments were performed using purified FLC spiked into normal serum to assess linearity and precision. In addition, a cohort of 27 patients with AL was analyzed and miRAMM was able to detect a monoclonal FLC in 23 of the 27 patients that had abnormal FLC values by immunonephelometry.<\/jats:p>\n                  <jats:p>The high resolution and high mass measurement accuracy provided by the mass spectrometry based methodology eliminates the need for \u03ba\/\u03bb ratios as the method can quantitatively monitor the abundance of the \u03ba and \u03bb polyclonal background at the same time it measures the monoclonal FLC.<\/jats:p>","DOI":"10.1515\/cclm-2015-0917","type":"journal-article","created":{"date-parts":[[2016,2,4]],"date-time":"2016-02-04T05:35:02Z","timestamp":1454564102000},"source":"Crossref","is-referenced-by-count":38,"title":["Monitoring free light chains in serum using mass spectrometry"],"prefix":"10.1515","volume":"54","author":[{"given":"David R.","family":"Barnidge","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Angela","family":"Dispenzieri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giampaolo","family":"Merlini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jerry A.","family":"Katzmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David L.","family":"Murray","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","reference":[{"key":"ref361","doi-asserted-by":"crossref","first-page":"1758","DOI":"10.1074\/mcp.M112.019620","article-title":"Analysis of intact monoclonal antibody IgG1 by electron transfer dissociation Orbitrap FTMS","volume":"11","year":"2012","journal-title":"Mol Cell 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chains","volume":"46","year":"2007","journal-title":"Biochemistry"},{"key":"ref01","first-page":"4","article-title":"Polyclonal free light chains: a biomarker of inflammatory disease or treatment target?","volume":"5","year":"2013","journal-title":"F1000 Med Rep"},{"key":"ref121","first-page":"356a","article-title":"Identification of amyloid proteins in formalin fixed paraffin embedded biopsy specimens by a novel method based on mass spectrometry following laser dissection and capture","volume":"87","year":"2007","journal-title":"Lab Invest"},{"key":"ref471","doi-asserted-by":"crossref","first-page":"9164","DOI":"10.1021\/ac401850p","article-title":"Unequivocal determination of site-specific protein disulfide bond reduction potentials by top-down FTICR MS: Characterization of the N- and C-terminal redox-active sites in human thioredoxin 1","volume":"85","year":"2013","journal-title":"Anal 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