Fracture of tendon collagen

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Abstract
A study of rat‐tail tendon fibers, about 200 μ in diameter, by scanning electron microscopy of fractured specimens reveals that these crimped fibers are largely made up of cylindrical units, about 10 μ in diameter. These, in turn, are made up of the well‐known collagen fibrils, ca. 0.1 μ in diameter, which have been observed previously by transmission electron microscopy and small‐angle x‐ray diffraction. Both the 10‐μ and 0.1‐μ cylindrical units were found to be arranged parallel to the macroscopic fiber axis rather than helically about it, as has been often proposed in the past. Significant improvement in resolution of the fracture surfaces was obtained by dehydration of the tendon. Microscopy of undehydrated tendon fibers undergoing solubilization by dilute aqueous acetic acid confirmed the results obtained by fractography.