Abstract
Currently used methods for investigating kinetics of peptide degradation such as refractive index monitoring, radioimmunoassay (RIA), high-performance liquid chromatography (HPLC), or capillary electrophoresis (CE) are time consuming, need large amounts of substrate, and are often too insensitive. Moreover, as in the case of RIA, HPLC, and CE, it is often impossible to interpret the observed results with confidence in the integrity of the analyte. To circumvent such obstacles, we found matrix-assisted laser desorption/ionization (MALDI) used with time-of-flight mass spectrometry (TOFMS) not only useful for qualitative analysis of reaction pathways but also for quantification. In the following chapter, we give two examples of kinetic reaction course evaluation, one non-enzymatic and one enzymatic.
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Rosche, F. et al. (2000). Kinetic Analysis of Enzymatic and Nonenzymatic Degradation of Peptides by MALDI-TOFMS. In: Chapman, J.R. (eds) Mass Spectrometry of Proteins and Peptides. Methods in Molecular Biology™, vol 146. Humana Press, Totowa, NJ. https://doi.org/10.1385/1-59259-045-4:251
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DOI: https://doi.org/10.1385/1-59259-045-4:251
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