Journal of Mass Spectrometry and Advances in the Clinical Lab最新文献

{"title":"Retraction notice to “Identification of metabolites of brexpiprazole in human urine for use in monitoring patient compliance” [Clin. Mass Spectrom. 6 (2017) 21–24]","authors":"Jeffrey R. Enders , Sandeep Gunna Reddy , Erin C. Strickland , Gregory L. McIntire","doi":"10.1016/j.jmsacl.2025.03.001","DOIUrl":"10.1016/j.jmsacl.2025.03.001","url":null,"abstract":"","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":"36 ","pages":"Page 82"},"PeriodicalIF":3.1,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143917545","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Quantification of total sBCMA in human plasma by peptide-level immunocapture LC-MS/MS","authors":"Johanna Paris ,&nbsp;Alexandra Tavernier ,&nbsp;Sylvie Bethegnies,&nbsp;Sandrine Descloux,&nbsp;Olivier Fedeli","doi":"10.1016/j.jmsacl.2025.04.006","DOIUrl":"10.1016/j.jmsacl.2025.04.006","url":null,"abstract":"<div><h3>Background</h3><div>B-cell maturation antigen (BCMA) is a membrane protein that is overexpressed in multiple myeloma cells and can be targeted with biotherapeutic agents. BCMA is naturally shed by γ-secretase, leading to the formation of soluble BCMA (sBCMA), which circulates in the blood. sBCMA can affect the efficacy of BCMA-targeted therapies and act as a drug sink. Additionally, sBCMA can interfere with pharmacokinetic measurements when BCMA is directly targeted. Therefore, quantification of this biomarker during clinical trials is essential to assess the effective dose and understand pharmacokinetic results. When quantifying sBCMA using ligand binding assays or hybrid assays, the biotherapeutic can interfere with the capture of sBCMA, leading to an underestimation of its levels.</div></div><div><h3>Methods</h3><div>Samples were denatured, reduced, and alkylated prior to trypsin digestion. sBCMA peptide enrichment was performed using anti-peptide polyclonal antibodies. Reversed-phase chromatographic separation was conducted on a biocompatible C18 column with an analysis time of sixteen minutes per sample. The SCIEX QTRAP 5500 mass spectrometer operated in multiple reaction monitoring mode. The calibration curve was prepared by spiking recombinant sBCMA into monkey plasma.</div></div><div><h3>Results</h3><div>The parallelism between the authentic and surrogate matrices, as well as between the endogenous and recombinant proteins, was validated. Comparisons were made between protein and peptide level hybrid assays, with the peptide level approach effectively removing the interference of the biotherapeutic. Additionally, the peptide level immunocapture LC-MS/MS demonstrated ligand tolerance.</div></div><div><h3>Conclusion</h3><div>The peptide level immunocapture LC-MS/MS analysis eliminated the interference of anti-BCMA biotherapeutics, allowing for the quantification of total sBCMA in clinical samples while achieving a LLOQ of 10 ng/mL.</div></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":"36 ","pages":"Pages 46-51"},"PeriodicalIF":3.1,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143859204","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A rapid method for determination of rosuvastatin in blood plasma with supported liquid extraction","authors":"Tjaša Dermota ,&nbsp;Mojca Božič Mijovski ,&nbsp;Jurij Trontelj","doi":"10.1016/j.jmsacl.2025.04.003","DOIUrl":"10.1016/j.jmsacl.2025.04.003","url":null,"abstract":"<div><h3>Introduction</h3><div>Accurate measurement of rosuvastatin in plasma is critical for effective patient management and treatment monitoring following myocardial infarction (MI). Expensive solid-phase extraction (SPE) and time-consuming liquid–liquid extraction (LLE) have been established for quantifying rosuvastatin. Supported liquid extraction (SLE) could offer a rapid, cost-effective alternative.</div></div><div><h3>Objectives</h3><div>This study aimed to develop and validate a rapid, cost-effective, accurate, and precise method for quantifying rosuvastatin in high-dose plasma samples from patients following MI.</div></div><div><h3>Methods</h3><div>Rosuvastatin was extracted from EDTA plasma using SLE and quantified with LC-MS/MS with positive electrospray ionization. The method was validated according to ICH M10 guidelines, focusing on selectivity, matrix effect, accuracy, precision, linearity, and carryover. Rosuvastatin-D6 was used as an internal standard. Additionally, thirty plasma samples from patients on high-dose rosuvastatin therapy (20 or 40 mg/day) following MI were analyzed by both LLE and SLE methods and compared.</div></div><div><h3>Results</h3><div>The method was successfully validated, demonstrating linearity across a range of 0.1 ng/mL to 50 ng/mL. Compared to the LLE method, SLE achieved superior extraction recovery (96.3 % vs. 60 %) and precision (RSD: 11.9 % vs. 13.6 %) at 0.3 ng/mL rosuvastatin, with a lower absolute matrix effect (12.7 % vs. −36.7 %). Accuracy was comparable (109.3 % vs. 92.8 %). Although SLE involves higher initial costs, it significantly enhances throughput, reduces solvent usage, and minimizes contamination and equipment wear.</div></div><div><h3>Conclusion</h3><div>This study validates SLE as a superior method for quantifying rosuvastatin in plasma, outperforming LLE in recovery, reproducibility, and automation. SLE offers greater accuracy and reliability, making it ideal for high-throughput applications.</div></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":"36 ","pages":"Pages 29-36"},"PeriodicalIF":3.1,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143820388","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development of an isotope dilution gas chromatography − mass spectrometry candidate reference measurement procedure for glucose in human serum","authors":"Komal Dahya ,&nbsp;Heather C. Kuiper ,&nbsp;Sarah W. Kingsley ,&nbsp;Uliana Danilenko ,&nbsp;Hubert W. Vesper","doi":"10.1016/j.jmsacl.2025.04.005","DOIUrl":"10.1016/j.jmsacl.2025.04.005","url":null,"abstract":"<div><h3>Introduction</h3><div>Diabetes is the seventh leading cause of death in the United States, impacting over 37 million people. Accurate glucose measurements are critical for effective diabetes management. A reliable candidate reference measurement procedure (cRMP) for assessing the analytical performance of glucose tests performed in patient care is essential for ensuring measurement accuracy.</div></div><div><h3>Methods</h3><div>We have developed a gas chromatography-mass spectrometry (GC–MS)-based cRMP for glucose in human serum. In this procedure, glucose is measured as the aldononitrile acetate derivative and quantitated using a ¹³C₆-glucose internal standard.</div></div><div><h3>Results</h3><div>Analytical selectivity was achieved through chromatographic separation and monitoring the quantitation ion/confirmation ion ratios in samples. With bias ranging from −0.79 % to 0.67 % for eight levels of serum-based certified reference materials from the National Institute of Standards and Technology (NIST) and Laboratoire national de métrologie et d’essais (LNE) and total CVs of 1.11 %, 0.68 % and 0.74 % at the low, medium, and high glucose concentration levels, respectively, the cRMP provided excellent accuracy and precision. The calibration curve was linear throughout the 13.51–378.21 mg/dL [0.75–21 mmol/L] measurement range (R² = 0.9999), with a mean slope of 270.73 (95 % CI, 270.19 to 271.27) and an intercept of 0.021 (95 % CI, −0.157 to 0.199). The limit of detection was 0.25 mg/dL (0.014 mmol/L) and the limit of quantitation was 0.83 mg/dL (0.046 mmol/L).</div></div><div><h3>Conclusion</h3><div>The described GC–MS method, with metrological traceability to the International System of Units (SI), provides highly accurate and precise measurements of glucose in human serum.</div></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":"36 ","pages":"Pages 63-72"},"PeriodicalIF":3.1,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143865047","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development and validation of a highly-sensitive, quantitative LC-MS/MS assay to evaluate plasma oxytocin","authors":"E. Grifnée ,&nbsp;A. Mackowiak ,&nbsp;J. Demeuse ,&nbsp;M. Schoumacher ,&nbsp;L. Huyghebaert ,&nbsp;W. Determe ,&nbsp;T. Dubrowski ,&nbsp;P. Massonnet ,&nbsp;S. Peeters ,&nbsp;G. Scantamburlo ,&nbsp;E. Cavalier ,&nbsp;C.Le Goff","doi":"10.1016/j.jmsacl.2025.02.002","DOIUrl":"10.1016/j.jmsacl.2025.02.002","url":null,"abstract":"<div><h3>Introduction</h3><div>Oxytocin is a 9-amino acid peptide that serves as neuromodulator in the human central nervous system. This peptide is implicated in the regulation of diverse behaviors and plays a significant role in positive social interaction. Currently, oxytocin levels are measured using immunoassays. However, these methods have several limitations that can lead to false results and erroneous interpretation. Given the remarkably low endogenous level of oxytocin in human plasma (low ng/L levels), we developed and rigorously validated a novel and highly sensitive LC-MS/MS method for oxytocin quantification in plasma.</div></div><div><h3>Methods</h3><div>Oxytocin was initially extracted using solid-phase extraction with an Oasis HLB 30 mg plate and then subjected to LC-MS/MS analysis. PBS-0.1 % BSA served as surrogate matrix for the preparation of validation samples and the calibration curve, ensuring no endogenous interference. The validation design followed the Clinical Laboratory Standards Institute guidelines. Precision, accuracy, and measurement uncertainty were determined using single-nested analysis of variance and e.noval software.</div></div><div><h3>Results</h3><div>A lower limit of quantification of 1 ng/L was achieved. The method was validated for oxytocin concentrations ranging from 1 ng/L to 75 ng/L, with precision (coefficient of variation) below 10 %, accuracy ranging from 94 % to 108 %, and measurement uncertainty below 15 %.</div></div><div><h3>Conclusion</h3><div>In this work, we developed and validated a highly sensitive LC-MS/MS method for the quantification of oxytocin in plasma. Our novel methodology is well-suited for clinical applications.</div></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":"36 ","pages":"Pages 19-28"},"PeriodicalIF":3.1,"publicationDate":"2025-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143510843","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Barcoded labels as potential source of zinc contamination in trace metal testing","authors":"Difei Sun ,&nbsp;Donna Sealy ,&nbsp;Dorothy Truong ,&nbsp;Danijela Konforte","doi":"10.1016/j.jmsacl.2025.02.003","DOIUrl":"10.1016/j.jmsacl.2025.02.003","url":null,"abstract":"","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":"36 ","pages":"Pages 9-10"},"PeriodicalIF":3.1,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143487604","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"MRM-based LC-MS method for accurate C-peptide quantitation","authors":"Will Grothoff,&nbsp;Ivan Khodakivskyi,&nbsp;Aleks Shin,&nbsp;Randie Little,&nbsp;Shawn Connolly,&nbsp;Kuanysh Kabytaev","doi":"10.1016/j.jmsacl.2025.02.001","DOIUrl":"10.1016/j.jmsacl.2025.02.001","url":null,"abstract":"<div><h3>Introduction</h3><div>C-peptide secretion mirrors beta-cell function and has emerged as a valuable clinical biomarker for diabetes mellitus. C-peptide measurements can provide estimates of insulin secretory capacity, aiding in clinical decision-making and differentiation between diabetes types. Unfortunately, C-peptide assays are still not standardized, which may limit their practical clinical use. We have developed an MRM-based LC-MS method that demonstrated accuracy close to our reference method.</div></div><div><h3>Objective</h3><div>To develop and validate a mass spectrometry method for accurate quantitation of C-peptide.</div></div><div><h3>Method</h3><div>A serum sample was spiked with isotope-labeled C-peptide as a standard. The enrichment process involved protein precipitation with methanol, solid-phase extraction, and anion exchange for C-peptide enrichment followed by Glu-C digestion. The peptide LGGGPGAGSLQPLALE was quantitated using MRM in positive ion mode. The calibration process includes C-peptide CRM material to ensure a complete traceability chain for the measurement.</div></div><div><h3>Results</h3><div>The assay exhibited linearity across a wide range of C-peptide concentrations and a limit of quantitation of 0.058 nmol/L. The inter-day imprecision was less than 9.6 % CV, and the intra-day imprecision was less than 8.9 % CV. Spiking with bilirubin, triglycerides, and hemoglobin demonstrated no interference, except for triglycerides at very high levels. The method exhibited a strong correlation to the C-peptide reference method (r2 = 0.95).</div></div><div><h3>Conclusion</h3><div>The developed mass spectrometry method has demonstrated accurate results in C-peptide quantitation and can serve as a supplemental method to the existing C-peptide reference method. This ensures sustained stability over time and ultimately refines the existing reference system.</div></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":"36 ","pages":"Pages 1-8"},"PeriodicalIF":3.1,"publicationDate":"2025-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143464384","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A multiplex assay of leptin, resistin, and adiponectin by immunoaffinity enrichment and targeted mass spectrometry","authors":"Jie Pu ,&nbsp;Xinxin Yang ,&nbsp;Tai-Tu Lin ,&nbsp;Thomas L. Fillmore ,&nbsp;Marina A. Gritsenko ,&nbsp;Shane S. Kelly ,&nbsp;Adam C. Swensen ,&nbsp;Tujin Shi ,&nbsp;Stephen R. Master ,&nbsp;James P. DeLany ,&nbsp;Bret H. Goodpaster ,&nbsp;Wei-Jun Qian ,&nbsp;Jun Qu","doi":"10.1016/j.jmsacl.2025.01.003","DOIUrl":"10.1016/j.jmsacl.2025.01.003","url":null,"abstract":"<div><h3>Background</h3><div>Leptin, resistin, and adiponectin are critical adipokines involved in the pathophysiology of obesity and its related disorders, including type 2 diabetes. Although these biomarkers have historically been quantified using immunoassays, the specificity of antibody-based methods has frequently been questioned. As a result, there is an increasing interest in developing reliable, multiplexed clinical assays that utilize mass spectrometry for improved accuracy. In this study, we present a multiplexed immunoaffinity liquid chromatography-tandem mass spectrometry (multi-IA-LC-MS/MS) assay designed for the sensitive and selective measurement of leptin, resistin, and adiponectin in human plasma.</div></div><div><h3>Methods</h3><div>Leptin, resistin, and adiponectin were selectively enriched from plasma samples using an antibody cocktail composed of monoclonal antibodies targeting each respective adipokine. The enriched adipokines underwent enzymatic digestion, and the resulting tryptic peptides were quantified using LC-MS/MS. The validated assay was subsequently applied to plasma samples collected from a cohort of subjects representing various weight categories, including normal weight, overweight, and obesity.</div></div><div><h3>Results</h3><div>The lower limits of quantification for the assay were determined to be 0.5 ng/mL for both leptin and resistin, and 50 ng/mL for adiponectin. Intra- day, inter- day, and total imprecision measurements were all &lt; 15 %, while spike recovery consistently exceeded 83 %. Comparative analysis with individual immunoassays demonstrated strong correlation, with all correlation coefficients (r) being equal to or greater than 0.869. Notably, when comparing subjects with obesity to those with normal weight, there was an approximately nine-fold increase in circulating leptin levels and a ∼1.6-fold decrease in circulating adiponectin levels.</div></div><div><h3>Conclusions</h3><div>A multi-IA-LC-MS/MS assay was developed for the simultaneous and sensitive measurement of leptin, resistin, and adiponectin in clinical samples. This quantitative method shows significant potential for applications related to obesity and could facilitate improved clinical management and understanding of obesity-related conditions.</div></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":"36 ","pages":"Pages 11-18"},"PeriodicalIF":3.1,"publicationDate":"2025-02-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143511099","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A liquid chromatography-high-resolution mass spectrometry method for separation and identification of hemoglobin variant subunits with mass shifts less than 1 Da","authors":"Ainslie Chen ,&nbsp;Ryan M. Aquino ,&nbsp;Hector A. Vidal ,&nbsp;Carolyn V. Wong ,&nbsp;Ruben Y. Luo","doi":"10.1016/j.jmsacl.2025.01.002","DOIUrl":"10.1016/j.jmsacl.2025.01.002","url":null,"abstract":"<div><h3>Background</h3><div>Identification of hemoglobin (Hb) variants is valuable in clinical testing. A common issue with conventional methods for identifying Hb variants is their subpar ability to provide structural breakdowns of the variants. Reports have surfaced of high-resolution mass spectrometry (HR-MS) methods that improve on traditional methods; however, ambiguities may arise without separation of Hb subunits prior to HR-MS analysis.</div></div><div><h3>Methods</h3><div>We report a liquid chromatography-high-resolution mass spectrometry (LC-HR-MS) method to separate several pairs of normal and variant Hb subunits with mass shifts of less than 1 Da and successfully identify them in intact-protein and top-down analyses. LC separation was facilitated by a C4 reversed-phase column.</div></div><div><h3>Results</h3><div>Seven heterozygous Hb variant samples (Hb C with α-thalassemia trait, Hb E, Hb D-Punjab, Hb G-Accra, Hb G-Siriraj, Hb Tarrant, and Hb G-Waimanalo) were selected to demonstrate the LC separation of Hb variant and normal subunits with mass shifts of less than 1 Da. The analytes could be explicitly observed in the deconvoluted MS¹ mass spectra. The top-down analysis matched the amino acid sequences of the correct Hb variant subunits.</div></div><div><h3>Conclusions</h3><div>The LC-HR-MS method described can effectively separate and identify Hb subunits, especially when the variant subunits have mass deviations of less than 1 Da from their corresponding normal subunits. With further evaluation to prove the clinical utility, the HR-MS methods including CE-HR-MS have the potential to complement or partially replace conventional methods of Hb variant identification in clinical laboratories.</div></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":"35 ","pages":"Pages 1-7"},"PeriodicalIF":3.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143171561","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"High-resolution mass spectrometry measurement of N-terminal carbamylated hemoglobin as a potential marker for chronic diseases with elevated blood urea levels","authors":"Fangjun Chen ,&nbsp;Priscilla S.-W. Yeung ,&nbsp;Carolyn V. Wong ,&nbsp;Ruben Y. Luo","doi":"10.1016/j.jmsacl.2025.01.001","DOIUrl":"10.1016/j.jmsacl.2025.01.001","url":null,"abstract":"<div><h3>Introduction</h3><div>N-terminal carbamylated hemoglobin (CarHb) reflects long-term blood urea levels and has potential as a marker for chronic kidney disease (CKD) and other chronic conditions with elevated blood urea levels. A liquid chromatography-high-resolution mass spectrometry (LC-HR-MS) method was developed to measure CarHb.</div></div><div><h3>Methods</h3><div>Apparent CarHb/Hb ratios were calculated from the peak area ratios of carbamylated to native N-terminal peptides digested from hemoglobin alpha and beta subunits. Blood samples from healthy individuals, CKD patients, and chronic obstructive pulmonary disease (COPD) patients were analyzed.</div></div><div><h3>Results</h3><div>The apparent CarHb/Hb ratios were significantly higher in CKD and COPD patients compared to healthy individuals. However, no significant differences were observed between the CKD and COPD patient groups.</div></div><div><h3>Conclusions</h3><div>In this study, an LC-HR-MS method was developed for quantifying the apparent CarHb/Hb ratios and exploring their potential for clinical diagnostic applications. CarHb is a promising marker for monitoring kidney diseases and other chronic conditions with elevated blood urea levels. Beyond CarHb, the use of other carbamylated proteins as clinical diagnostic and prognostic markers can be explored.</div></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":"35 ","pages":"Pages 8-13"},"PeriodicalIF":3.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143360671","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}