Journal
CLINICA CHIMICA ACTA
Volume 492, Issue -, Pages 91-94Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.cca.2019.02.017
Keywords
MALDI-TOF mass spectrometry; Monoclonal immunoglobulin; Multiple myeloma; Daratumumab
Categories
Funding
- Society of Memorial Sloan Kettering Cancer Center
- Memorial Sloan Kettering Core Grant [P30 CA008748]
- National Cancer Institute
Ask authors/readers for more resources
Background: Daratumumab, a therapeutic IgG kappa monoclonal antibody, can cause a false positive interference on electrophoretic assays that are routinely used to monitor patients with monoclonal gammopathies. In this study, we evaluate the ability of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to distinguish daratumumab from disease-related IgG kappa monoclonal proteins (M-protein). Methods: Waste clinical samples from 31 patients who were receiving daratumumab and had a history of IgG kappa monoclonal gammopathy were collected. Immunoglobulins were purified from serum and analyzed by MALDI-TOF MS. Mass spectra were assessed for the presence of distinct monoclonal proteins. For samples in which only one monoclonal peak was identified near the expected m/z of daratumumab, the Hydrashift 2/4 Daratumumab Assay was used to confirm the presence of an M-protein. Results: Using MALDI-TOF MS, daratumumab could be distinguished from M-proteins in 26 out of 31 samples (84%). Results from 2 samples were inconclusive since the M-protein was not detected by the Hydrashift assay and may also be undetectable by MALDI-TOF MS. Comparatively, daratumumab was distinguishable from M-proteins in 14 out of 31 samples (45%) by immunofixation. Conclusions: MALDI-TOF MS offers greater specificity compared to immunofixation for distinguishing daratumumab from M-proteins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available