Article ID Journal Published Year Pages File Type
2420569 Animal Feed Science and Technology 2008 13 Pages PDF
Abstract

The digestion of dietary protein bound by condensed tannins (CTs) in ruminants was investigated by determining the extent of dissociation of insoluble 125I-BSA + CT complexes administered to abomasally and intestinally fistulated sheep. The extent of dissociation was registered as the true digestibility of iodinated bovine serum albumin (125I-BSA). The true digestibility of 125I-BSA originally bound to Leucaena pallida CT (0.721) was lower (P<0.05) than that of 125I-BSA originally bound to L. leucocephala CT (0.880) between the abomasum and terminal ileum. These results indicate that differences in the ability of CT to inhibit 125I-BSA digestion in vivo matched the relative abilities of the same CT to bind BSA in vitro, indicating that the in vitro BSA-binding assay for ranking CT behaviour was biologically relevant in vivo. Furthermore, the true digestibility of CT-bound 125I-BSA between the mouth and faeces permitted the prediction of the quantitative contribution that CT-bound dietary proteins make to improved nitrogen supply to the small intestines.

Related Topics
Life Sciences Agricultural and Biological Sciences Animal Science and Zoology
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