https://www.selleckchem.com/products/emd638683.html High throughput process technology studies were conducted to optimise binding and elution conditions for multi modal cation exchanger, Capto™ MMC and strong anion exchanger Capto™ Q. A dynamic binding capacity of 14 mg ml-1 was achieved for Capto™ MMC resin. Samples derived from each purification process were thoroughly characterized by RP-HPLC, SEC-HPLC, SDS-PAGE and LC-ESI-MS/MS Mass Spectrometry analytical methods. Modular polyomavirus major capsid protein could be purified within hours using the optimised process achieving purities above 87% and above 96% with inclusion of an initial precipitation step. Purified capsid protein could be easily assembled in-vitro into well-defined virus-like particles by lowering pH with addition of calcium chloride to the eluate. High throughout studies allowed the screening of a vast design space within weeks, rather than months, and unveiled complicated binding behaviour for CaptoTM MMC.An analytical approach using high-performance liquid chromatography-tandem mass spectrometry (LC-MS/MS) was developed to simultaneously detect Fagopyrum esculentum Moench (buckwheat) and cereals containing gluten (Triticum species including wheat and spelt, rye, barley, and oats) that were specified in regulations for food allergen labeling on processed foods. Trypsin-digested peptides were purified from different processed food commodities and heptapeptides derived from buckwheat 13S globulin (GFIVQAR, m/z 395.8 [precursor] > 177.0 [product]) and Triticum low molecular weight glutenin (QIPEQSR, m/z 429.3 [precursor] > 616.2 [product]) were specifically detected each species at levels as low as 0.050-0.056 µg/L and 0.028-0.032 µg/L, respectively. Detection of these synthetic peptides was quantitative to over 100 µg/L by reference to the synthetic peptide calibration curves and at recovery rates, 76.6 ± 4.1%-104.8 ± 17.1% and 82.4 ± 2.0%-105.8 ± 5.3%, for GFIVQAR and QIPEQSR, respectively, when