RESUMO
Non-enzymatic glycosylation of rat tail tendon collagen was examined by incubation with D-glucose in vitro. The changes in molecular parameters such as viscosity, thermal stability, electrophoretic mobility and solubility were determined on nonenzymatically glycosylated collagen in vitro. Tendons incubated with 8 and 24 mg glucose/ml showed an increase in dissolution temperature and a l·6-3-fold increase in thermal isometric tension respectively when compared to tendons incubated in the absence of glucose, indicating the formation of new intermolecular bonds. This conclusion was further supported by the decreased solubility of glycosylated collagen in 0·5 Ν acetic acid and the change in sub-unit composition as measured from the sodium dodecyl sulphate Polyacrylamide gel electrophoresis pattern. Glycosylated collagen gave a characteristic absorption spectra (λmax 248 nm) as distinct from that of control (λmax 242 nm). Denaturation temperature of glycosylated collagen, as determined from temperature dependent viscosity measurements, was reduced. These studies indicate that glycosylation affects the molecular interactions as well as the crosslinking of collagen.