AI Article Synopsis
- Collagens are the most abundant proteins in mammals and contain a significant amount of specific hydroxylated amino acids, including various forms of hydroxyproline and hydroxylysine.
- A new method using RPC-UV-ESI-MS allows for the simultaneous separation and analysis of all five hydroxyamino acids along with two hydroxyproline epimers after transforming them with a chemical derivative.
- This technique has been successfully applied to different peptides containing hydroxyproline and collagen type I, demonstrating its versatility and effectiveness.
Article Abstract
Collagens, the most abundant mammalian proteins, contain a high content of hydroxylated amino acids, such as, 3- and 4-cis-/trans-hydroxyproline (Hyp) and 5-hydroxylysine (Hyl). Whereas the global content of 4-Hyp was studied by amino acid analysis, no technique to determine all five hydroxyamino acids simultaneously in collagens has been reported. Here, we report the separation of all five hydroxyamino acids as well as two Hyp epimers from all other proteinogenic amino acids after derivatization with N(2)-(5-fluoro-2,4-dinitrophenyl)-l-valine amide (l-FDVA) by RPC-UV-ESI-MS. The general applicability of this method is shown for three Hyp-containing peptides as well as collagen type I.
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| http://dx.doi.org/10.1016/j.jchromb.2006.10.015 | DOI Listing |
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