Jam. Ramshaw et al., METHYLENE-BLUE SENSITIZED PHOTOOXIDATION OF COLLAGEN FIBRILS, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1206(2), 1994, pp. 225-230
Isometric tension measurements on rat tail tendons showed that visible
light in the presence of Methylene blue led to an increase in the the
rmal stability of the collagen. Analysis of CNBr fragments by SDS-poly
acrylamide gel electrophoresis showed a decrease in the amounts of low
molecular weight fragments and an increase in the formation higher mo
lecular components with irradiation time. Amino-acid analysis data ind
icated that the relative yields of only tyrosine, methionine and histi
dine were reduced by the irradiation, with the loss of histidine being
the greatest. The loss of methionine was not sufficient to completely
account for the increases in the CNBr fragment sizes. Comparable resu
lts were also obtained with ultra-violet light. These thermal and chem
ical data were interpreted as being due to the formation of new interm
olecular cross-links in the tendon collagen. X-ray fibre diffraction s
howed that the irradiation and the induced cross-linking did not lead
to a substantial change or disorder in the molecular packing arrangeme
nt within the native collagen