Electron-microscopic study of the collagen fibrils of the rat tail tendon as revealed by freeze-fracture and freeze-etching techniques

Abstract

The ultrastructure of the collagen of rat tail tendon was investigated by the freeze-fracture technique. Collagen fibers were pretreated with the digestive enzymes, alpha-amylase, elastase and collagenase to remove matrix substances. Some of the samples were etched for 20 min. Fibrils had an average diameter of 318 +/- 12 nm and a banded structure with a mean periodicity of 64.2 +/- 0.9 mm; the banding was most marked in alpha-amylase/elastase-treated specimens, although the periodicity was independent of pretreatment. Microfibrils were well-displayed following alpha-amylase/elastase and collagenase pretreatments. A difference in the diameters of microfibrils was, however, observed between etched specimens (8.3 +/- 0.3 nm) and those prepared by other experimental methods (11.4 +/- 0.5 nm). In replicas of collagenase-treated and etched specimens, the interconnecting filaments in the interfibrillar region formed a network that was continuous with the microfibrils of collagen fibrils. The diameter of the interconnecting filaments was the same as that of microfibrils. Microfibrillar bundles were observed in the interfibrillar region.