Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 532000
Title An isotope dilution model for partitioning of phenylalanine and tyrosine uptake by the liver of lactating dairy cows
Author(s) Crompton, L.A.; Mcknight, L.L.; Reynolds, Chris; Mills, J.A.N.; Ellis, J.L.; Hanigan, M.D.; Dijkstra, J.; Bequette, B.J.; Bannink, A.; France, J.
Source Journal of Theoretical Biology 444 (2018). - ISSN 0022-5193 - p. 100 - 107.
DOI https://doi.org/10.1016/j.jtbi.2017.12.016
Department(s) LR - Animal Nutrition
Animal Nutrition
WIAS
Publication type Refereed Article in a scientific journal
Publication year 2018
Keyword(s) Isotope dilution - Kinetic model - Liver - phenylalanine - Tyrosine
Abstract An isotope dilution model to describe the partitioning of phenylalanine (PHE) and tyrosine (TYR) in the bovine liver was developed. The model comprises four intracellular and six extracellular pools and various flows connecting these pools and external blood. Conservation of mass principles were applied to generate the fundamental equations describing the behaviour of the system in the steady state. The model was applied to datasets from multi-catheterised dairy cattle during a constant infusion of [1-13C] phenylalanine and [2,3,5,6-2H] tyrosine tracers. Model solutions described the extraction of PHE and TYR from the liver via the portal vein and hepatic artery. In addition, the exchange of free PHE and TYR between extracellular and intracellular pools was explained and the hydroxylation of PHE to TYR was estimated. The model was effective in providing information about the fates of PHE and TYR in the liver and could be used as part of a more complex system describing amino acid metabolism in the whole animal.
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