%0 Journal Article %A Huiyan Li %A Robert Popp %A Christoph H. Borchers %T Affinity-mass spectrometric technologies for quantitative proteomics in biological fluids %D 2017 %R 10.1101/114751 %J bioRxiv %P 114751 %X Proteins are the functional molecules in organisms and are therefore excellent biomarker candidates for a diversity of diseases. Immunoassays and mass spectrometry (MS) are two major technologies being used in proteomics; however, they either lack specificity or sensitivity. An emerging trend is to combine immunoassays with MS (which we call “affinity-MS”). This is an important milestone in quantitative proteomics, making it possible to measure low-abundance proteins with high specificity. The targeted enrichment and the assignment of mass-to-charge ratios to different molecules provide two selection criteria, making affinity-MS highly specific. Picogram-per-milliliter limits of detection have been obtained for many proteins. Furthermore, multiplexing capacity of >150 proteins has been achieved. This article reviews different formats of affinity-enrichment methods, and demonstrates how they are interfaced with both electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) MS. The pros and cons of these techniques are compared, and future prospectives are discussed. %U https://www.biorxiv.org/content/biorxiv/early/2017/03/08/114751.full.pdf