Abstract
Collagen fibrils from different rat tendons have been investigated by freeze-fracture and transmission electron microscopy. In all cases, marked differences in both fibril morphology and subfibrillar organisation have been consistently found between the tendon core (composed of large and heterogeneous fibrils comprising tightly-packed, straight, parallel molecules) and sheath (showing small, uniform collagen fibrils with a helical arrangement of the molecules). The bio-mechanical requirements to which these tissues are subjected suggest, as do previous observations on other tissues, that a causal correlation exists between substructure and collagen fibril function.
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