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- W1983447062 abstract "1.1. The intra- and intermolecular cross-linking characteristics of collagen isolated from the intramuscular connective tissues of ovine, bovine, and porcine l. dorsi muscles were investigated.2.2. Species differences in extent of synthesis and intermolecular cross-linking were observed.3.3. No difference in α/β ratio was found in the salt-soluble fractions, but bovine collagen had a significantly lower β12/ β11 ratio than ovine or porcine.4.4. In the acid-soluble fractions, porcine samples had 64 per cent dimer subunits, while ovine had 55 per cent and bovine 53 per cent. The greatest increase in the dimer content of the porcine samples was in the β12 fraction.5.5. The thermal shrinkage temperature of porcine muscle collagen was also significantly lower (P<0.01) than that from the other species.6.6. Only slight differences between species were found in amino-acid composition." @default.
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- W1983447062 date "1971-04-01" @default.
- W1983447062 modified "2023-09-27" @default.
- W1983447062 title "Species variation in the cross-linking characteristics of collagen from the intramuscular connective tissues of striated muscles (Bos taurus, Ovis aries, Sus scrofa)" @default.
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- W1983447062 doi "https://doi.org/10.1016/0020-711x(71)90207-2" @default.
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