About: Hydroxyproline is a research topic. Over the lifetime, 3312 publications have been published within this topic receiving 111087 citations. The topic is also known as: 4-hydroxyproline & Hypro.
TL;DR: Method has been applied to a study of hydroxyproline distribution in cell particulates, tissue fluids, and purified plant and animal proteins, and significant amounts of hydroXYproline were found in crystalline preparations of pepsin, elastase.
TL;DR: Measurements on several dipeptides showed that proline peptide do not form ultraviolet-absorbing complexes with copper whereas prolyl peptides do form such complexes, which explains the finding that gelatin (which has a high proportion of proline and of hydroxyproline residues) is less reactive with copper than are the other proteins studied here.
TL;DR: A short and simple calorimetric method is here described that is applicable to the determination of hydroxyproline in hydrolysates of 40 to 100 y of collagen with a reproducibility of f2 per cent and an accuracy of f1 per cent as judged by recovery of hydroXYproline from elastin hydrolysate and from an amino acid mixture simulating collagen.
TL;DR: The modified hydroxyproline assay presented in this communication will be useful for routine measurement of collagen content in extracts of various tissue specimens and can be used for batch processing of column fractions to monitor the collagen concentrations during purification.
TL;DR: The findings of this study suggest that various biomaterials support the chondrogenic differentiation of hADAS cells, and that manipulating the composition of these tissue engineered constructs may have significant effects on their mechanical properties.