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Updated: May 27, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
Published on: September 20, 2012
Pyridinoline in ovine intramuscular collagen
O A Young1, T J Braggins, G J Barker
1Meat Industry Research Institute of New Zealand (Inc.), PO Box 617, Hamilton, New Zealand.
Abstract:
Pyridinoline, a mature crosslink of collagen, was measured in intramuscular connective tissue isolated from ovine semimembranosus, a muscle noted for its highly insoluble collagen. Concentration ranged between 0·25 and 0·59 mol/mol of collagen, on the high side of concentrations reported in the literature for this and other muscles in various species. Pyridinoline concentration was inversely related to collagen solubility in muscle homogenates (P < 0·0). In a comparison between semimembranosus, biceps femoris and gluteus medius, pyridinoline concentration was again inversely related to collage solubility. For all these muscles, pyridinoline remained insoluble in a heat-dependent solubility test, but it is argued that pyridinoline does not explain all the solubility properties of ovine intramuscular collagen. Pyridinoline concentration was not significantly correlated with sensory or shear properties of cooked semimembranosus, confirming the importance of other heat-stable crosslinks.
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