Artigo Revisado por pares

Pyridinoline in ovine intramuscular collagen

1994; Elsevier BV; Volume: 37; Issue: 2 Linguagem: Inglês

10.1016/0309-1740(94)90088-4

ISSN

1873-4138

Autores

O.A. Young, Terry J. Braggins, George Barker,

Tópico(s)

Osteoarthritis Treatment and Mechanisms

Resumo

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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