Changes

Stable aggregations of collagen molecules to form fibrils are achieved by cross-linking of the molecules.  These give collagen both strength and elasticity.  In newly formed collagen, the cross-links are relatively few, but with age, there is a significant increase in the number and the stability of the cross-links.  This has two significant effects.  Excessive stress on immature collagen contributes to tendon and ligament disease in young animals; the training of horses especially must take the aging of collagen into account.  Also, variations in collagen cross-links cause the toughness associated with different cuts of meat, and with the increase in toughness in meat from older animals.

Stable aggregations of collagen molecules to form fibrils are achieved by cross-linking of the molecules.  These give collagen both strength and elasticity.  In newly formed collagen, the cross-links are relatively few, but with age, there is a significant increase in the number and the stability of the cross-links.  This has two significant effects.  Excessive stress on immature collagen contributes to tendon and ligament disease in young animals; the training of horses especially must take the aging of collagen into account.  Also, variations in collagen cross-links cause the toughness associated with different cuts of meat, and with the increase in toughness in meat from older animals.

[[File:QMSection2.10.png|thumb|'''Fig. 2.10 Collagen cross-links''']]

[[File:QMFig 2.10.jpg|thumb|'''Fig. 2.10   Collagen cross-links''']]

:::::'''Fig. 2.10   Collagen cross-links'''

:::::'''Fig. 2.10   Collagen cross-links'''