Abstract
Hydroxyproline (Hyp) is an imino acid post-translationally formed by sequence-specific hydroxylases in the repeating collagen Gly–Xaa–Yaa triad present in all collagen types of all species. In both Xaa- and Yaa-positions, Pro is the most common residue, often oxidized to 4-Hyp in the Yaa- and rarely to 3-Hyp in the Xaa-positions. Here, we describe the qualitative and quantitative analysis of 3- and 4-Hyp-isomers by separating the free imino acids either with hydrophilic interaction chromatography (HILIC) or after derivatization with reversed-phase chromatography (RPC). In both cases, the compounds were detected by electrospray ionization mass spectrometry (ESI-MS).
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Langrock, T., Hoffmann, R. (2012). Analysis of Hydroxyproline in Collagen Hydrolysates. In: Alterman, M., Hunziker, P. (eds) Amino Acid Analysis. Methods in Molecular Biology, vol 828. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-445-2_21
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DOI: https://doi.org/10.1007/978-1-61779-445-2_21
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