Scientist Cornelia Kasper and colleagues from the Gottfried Wilhelm Leibniz University of Hanover (Hanover, Germany) thought that a liquid chromatography method with short monolithic columns would be a quicker alternative to measure proteins in culture while also having had the potential to separate different proteins.
Scientist Cornelia Kasper and colleagues from the Gottfried Wilhelm Leibniz University of Hanover (Hanover, Germany) thought that a liquid chromatography method with short monolithic columns would be a quicker alternative to measure proteins in culture while also having had the potential to separate different proteins. They targeted immunoglobulin G (IgG), insulin, and transferrin, which are regularly encountered in cultures. Kasper realised that one column would not separate these three proteins due to their different properties. So, they joined two types of monolithic column in one housing in a prep HPLC station with UV (280 nm) and conductivity detectors. The first was a monolithic affinity disk in which protein G was immobilised on to convective interaction media (CIM) epoxy disks whereas the second was a monolithic quaternary ammonium (QA) CIM disk. Each disk was just 12 mm x 3 mm in size with a bed volume of 0.34 mL.
The results proved the viability of the method in general. Kasper declared that the availability of monolithic disks of different material and surface chemistries, along with other immobilised proteins, allows the technique to be extended to other analyses. It could be used to track protein purification processes and determine the quality and purity of separated proteins. For cell cultures or other biological media such as plasma, rapid, and simultaneous analysis of several proteins has just been made possible.
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