title: Analysis of hydroxyproline in collagen hydrolysates.
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).
authors: Institute of Bioanalytical Chemistry, Faculty of Chemistry and Mineralogy and Center for Biotechnology and Biomedicine, Universität Leipzig, Leipzig, Germany.
authors: Tobias
authors: T
authors: Langrock
authors: Ralf
authors: R
authors: Hoffmann
mesh_terms: D000818:Animals; D002851:Chromatography, High Pressure Liquid; D056148:Chromatography, Reverse-Phase; D003094:Collagen / Q000737:chemistry*; D005740:Gases; D006801:Humans; D006868:Hydrolysis; D057927:Hydrophobic and Hydrophilic Interactions; D006909:Hydroxyproline / Q000032:analysis* / Q000737:chemistry; D007536:Isomerism
chemical_list: D005740:Gases; D003094:Collagen; D006909:Hydroxyproline