Physical and Physical-Chemical Heterogeneity of Collagen Fibres from Rat Tail Tendon

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Abstract
Physical (tensile strength and elasticity) and physical-chemical properties of collagen fibers (chemical contraction and relaxation and binding of Ca) from the rat tail tendon do not depend only on the diameter of the isolated fiber, but on its topographic location in the tendon. Fiber diameter increases towards the upper part of the tail. From fibers of the same diameter, isolated from the 3 different parts of the tendon, fibers of the proximal part have a greater tensile strength elasticity and linkage ability for Ca and smaller contraction and relaxation ability in 2.5 M NaClO4. The diameter of the proximal part of the same fiber is greater. This part is stronger and more extensible. This finding confirms the different arrangements of the ultrastructure and the equal action of the binding forces along the whole collagen fiber. The optimum of the increasing strength velocity of loading was fixed for the determination of the tensile strength and elasticity. The diminishing of the normal hydration of the fiber does not influence the tensile strength and elasticity. The ontogenetic process of the changes of the tensile strength of collagen fibers was determined.

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