- Day 2, May 16（Thu.） 09:30-09:50 Room C (101)
Native Mass Spectrometry of Proteins and DNA Prepared under Quasi-Physiological Conditions
Native mass spectrometry (Native MS) with nanoESI enabled observation of intact ions of protein complexes with a small amount of sample. It is possible to definitely determine the binding stoichiometry of protein complexes without difficulty. However, samples for native MS are basically required to prepare in volatile solutions, such as aqueous ammonium acetate. In the present study, we could observe intact ions of G-quadruplex DNA prepared in potassium phosphate buffer, without any solvent exchange prior to MS measurement, by optimizing the nanoESI-sprayer shape and measurement conditions. Furthermore, we succeeded in observation of intact ions of recombinant dihydrofolate reductase (DHFR) associated with NADPH, without any purification procedures from the cell lysate.