AI Article Synopsis
- Hydroxyproline (Hyp) is an imino acid found in collagen, formed by specific hydroxylases in a repeating triad structure of collagen across all species.
- In collagen, the most common residues at the Xaa and Yaa positions are proline, which can be oxidized to form either 4-Hyp or rarely 3-Hyp.
- This study focuses on the analysis of 3- and 4-Hyp isomers using hydrophilic interaction chromatography (HILIC) and reversed-phase chromatography (RPC), with detection done through electrospray-ionization mass spectrometry.
Article Abstract
Hydroxyproline (Hyp) is an imino acid posttranslationally 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.
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| http://dx.doi.org/10.1007/978-1-4939-9639-1_5 | DOI Listing |
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