Determination of collagen degradation products in human urine in osteoarthrosis

A new method for profiling human urine has been developed. Peptides of molecular weight greater than 10,000 were separated by high-performance liquid chromatography with fluorescence monitoring (excitation 297 nm, emission filter 389 nm) adjusted for detection of collagen cross-linking compound pyridinoline. The collagen origin of some peptides was confirmed by determination of hydroxyproline in their hydrolysates. Peak heights were substantially higher in patients with osteoarthrosis than at healthy controls. After replacement of the diseased joint by total endoprosthesis the chromatograms changed and were similar to those of healthy controls.