Monitoring the fate of dietary proteins in rumen fluid using gel electrophoresis
1988
Spencer, D. | Higgins, T.J.V. | Freer, M. | Dove, H. | Coombe, J.B.
When fractionated by sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE), strained rumen fluid from sheep fed on pelleted lucerne (Medicago sativa) hay showed no major protein components that stain with Coomassie Blue. This feature made it possible to monitor the fate of individual polypeptides within a protein mixture incubated in rumen fluid in vitro. Extracts from a number of seed meals (sunflower (Helianthus annuus)), lupin (Lupinus angustifolius)), rape (Brassica napus) and pea (Pisum sativum L.), as well as casein and bovine serum albumin, were examined in this system. The protein components of each seed type showed a wide range of resistances to degradation. One protein in pea seeds (pea albumin 1), which is particularly rich in cysteine, was almost as resistant to rumen degradation as bovine serum albumin. Analysis of synthetic-fibre-bag experiments by SDS-PAGE showed that the rate of loss of total protein from solid meal residues does not provide an index of the resistance of individual protein components of the meal to rumen degradation. While there was no qualitative change in the protein profile of residual pea-seed meal inside a synthetic-fibre bag, there was considerable variation in the rate at which individual, solubilized protein components were degraded in the surrounding rumen fluid.
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