Differences in the fibril structure of corneal and tendon collagen. An electron microscopy and X-ray diffraction investigation.
A detailed analysis of the D-period and axial electron density distribution of cornea and tendon collagen was carried out by means of X-ray diffraction and electron microscopy. Ultrastructural observations were made on replicas of freeze fractured and deep-etched specimens. Synchrotron radiation was used to obtain high resolution small angle X-ray diffraction patterns. The data provide evidence that D-period and intraperiod distances in cornea are shorter than in tendon collagen fibrils. The observed different banding observed is interpreted on the basis of the different morphological arrangement of the microfibrils in the two tissues: "helicoidal" in cornea and "straight" in tendon microfibrils.
D000818:Animals; D003094:Collagen / Q000378:metabolism*; D003315:Cornea / Q000378:metabolism* / Q000648:ultrastructure; D005614:Freeze Fracturing; D046911:Macromolecular Substances; D008854:Microscopy, Electron / Q000379:methods; D009928:Organ Specificity; D051381:Rats; D011919:Rats, Inbred Strains; D013710:Tendons / Q000378:metabolism* / Q000648:ultrastructure; D014961:X-Ray Diffraction / Q000379:methods
D046911:Macromolecular Substances; D003094:Collagen