ArticleRapid communications in mass spectrometry : RCM2011
Selected reaction monitoring (SRM) mass spectrometry without isotope labeling can be used for rapid protein quantification.
Article in Rapid communications in mass spectrometry : RCM, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- A label-free selected reaction monitoring workflow identifies a subset of pregnancy specific glycoproteins as potential predictive markers of early-onset pre-eclampsia.Molecular & cellular proteomics : MCP · 2013Trial
- Label-Free Targeted Proteomics Data Analysis Workflow Selection - Benchmarking AI-based and Data-Driven Approaches.Molecular & cellular proteomics : MCP · 2026Article
- Mass spectrometry-based proteomics of FFPE tissues: progress, limitations, and clinical translation barriers.Clinical proteomics · 2025Review
- New ionization tags based on the structure of the 5-azoniaspiro[4.4]nonyl tag for a sensitive peptide sequencing by mass spectrometry.Analytical and bioanalytical chemistry · 2018Article
- Nitric oxide mediated inhibition of antigen presentation from DCs to CD4Scientific reports · 2017Article
- Proteomics progresses in microbial physiology and clinical antimicrobial therapy.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2017Review
- Early biomarkers of joint damage in rheumatoid and psoriatic arthritis.Arthritis research & therapy · 2015Review
- Immunologic and mass-spectrometric estimates of SHBG concentrations in healthy women.Metabolism: clinical and experimental · 2014Article
- Immunological and mass spectrometric assays of SHBG: consistent and inconsistent metabolic associations in healthy men.The Journal of clinical endocrinology and metabolism · 2014Article
- A caspase-3 'death-switch' in colorectal cancer cells for induced and synchronous tumor apoptosis in vitro and in vivo facilitates the development of minimally invasive cell death biomarkers.Cell death & disease · 2013Article
- Arabidopsis peroxisome proteomics.Frontiers in plant science · 2013Article
- Identification of differentially expressed proteins in direct expressed prostatic secretions of men with organ-confined versus extracapsular prostate cancer.Molecular & cellular proteomics : MCP · 2012Article
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3 authors.
Funding
Abstract
The validation of putative biomarker candidates has become the major bottle-neck in protein biomarker development. Conventional immunoaffinity methods are limited by the availability of antibodies and kits. Here we demonstrate the feasibility of using selected reaction monitoring (SRM) without isotope labeling to achieve fast and reproducible quantification of serum proteins. The SRM/MRM assays for three standard serum proteins, including ceruloplasmin (CP), serum aymloid A (SAA) and sex hormone binding globulin (SHBG), have good linear ranges, generally 10(3) to 10(4) . There are almost perfect correlations between SRM intensities and the loaded peptide amounts (R(2) is usually ~0.99). Our data suggest that SRM/MRM is able to quantify proteins within the range of 0.2-2 fmol, which is comparable to the commercial ELISA/LUMINEX kits for these proteins. Excellent correlations between SRM/MRM and ELISA/LUMINEX assays were observed for SAA and SHBG (R(2)=0.928 and 0.851, respectively). However, the correlation between SRM/MRM and ELISA for CP is less desirable (R(2)=0.565). The reproducibility for SRM/MRM assays is generally very good but may depend on the proteins/peptides being analyzed (R(2)=0.931 and 0.882 for SAA and SHBG, and 0.723 for CP). The SRM/MRM assay without isotope labeling is a rapid and useful method for protein biomarker validation in a modest number of samples and is especially useful when other assays such as ELISA or LUMINEX are not available.
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