Proteins are traditionally quantified using bottom-up techniques, which involve enzymatic digestion of the target protein into constituent peptides.  In order to reduce sample preparation steps, we developed means to perform multiple reaction monitoring on a triple quadrupole mass spectrometer for the top-down quantification of intact proteins.  The key is in tuning the collision energy to generate a small number of unique and reproducible product ions.  We have further evaluated ion transmission properties of protein ions in the mass spectrometer.  In the context of intact protein quantitation, we believe there are some useful adjustments and data treatment strategies that can significantly enhance protein ion detection using triple quadrupole mass spectrometry, relative to what is commonly done for small molecules on such instruments.<br/>

Targeting intact proteins using triple quadrupole mass spectrometry

254th National Meeting (2017)

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