Abstract
Our identification of a family of genetically distinct collagens specifically distributed in the connective tissue of muscle now poses questions on their possible role in myoblast differentiation, muscle development, turnover and function in the living muscle, and post-rigor in the tenderness of meat. Using collagen-type specific antibodies we have shown temporal transitions in the type of collagen synthesized during myogenesis. Similar temporal transitions are currently being observed during muscle development. Immunofluorescence techniques also indicated that collagen did not play a role in muscle pattern formation. Once the muscle pattern has been established, the specific distribution of the collagen types in the endo-mysium (IV and V), perimysium (III and I) and epimysium (I) is maintained during growth. Using an arrested growth model we demonstrated that there was no significant loss of the pre-existing collagen, indicating that the mature collagen fibers do not restrict growth. As the growth rate decreased and the animal matures, the collagen fibers, initially stabilized by intermolecular head-to-tail cross-links, form a stable network via multivalent cross-links. These cross-links determine the extent of the tension generated during heating and the residual adhesion between muscle fibers and hence, the greater the proportion present the tougher the meat. It is therefore the quality rather than the quantitiy of the collagen that determines its contribution to the texture of meat.

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