Abstract
The acid solubility of the collagen of cockerel tendon demonstrates a similar degree of intermolecular acid-labile cross-linkage to that found in adult human tendon, implying similar maturity of the collagen. By contrast, rabbit tendon collagen demonstrates a dissimilar degree of cross-linkage suggesting immaturity of the collagen. Since this cross-linkage is likely to be related to mechanical properties, the cockerel may well be a better animal model than the rabbit for the study of tendon healing.
The application of ultrasound to sutured cockerel tendons produced no change in the mechanical strength of the tendon at six weeks, or its propensity to form adhesions, relative to untreated control sutured tendons. This contrasts with the decrease in strength after ultrasound found by previous workers using rabbits.
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