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An Evaluation of Postabsorptive Protein and Amino Acid Metabolism in the Lactating Dairy Cow
The current protein system utilized in the US was formulated in 1985 with minor modifications in 1989 and has gained widespread acceptance. However, some of the assumptions that were adopted by the National Research Council (NRC) appear to be inconsistent with observational data. The marginal effici...
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Published in: | Journal of dairy science 1998-12, Vol.81 (12), p.3385-3401 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The current protein system utilized in the US was formulated in 1985 with minor modifications in 1989 and has gained widespread acceptance. However, some of the assumptions that were adopted by the National Research Council (NRC) appear to be inconsistent with observational data. The marginal efficiency of conversion of absorbed protein to milk protein was assumed by NRC to be 70% until the requirement for absorbed protein was met and was 0% thereafter. The mean marginal efficiency observed for abomasal casein infusions reported in the literature and collected at the Purina Mills Research Center was 21%. Sorting the data into protein-sufficient and protein-deficient classes did not support the assumptions of 70% marginal efficiency in a deficient state and 0% marginal efficiency in the sufficient state. Analyses of nitrogen balance data and abomasal flow data and the work of Van Straalen et al. (77) indicated that energy status of the animal plays a role in determining the response to absorbed protein. Such a consideration was not included in the NRC model. The adoption of equations that describe metabolism at the organ level as opposed to the animal level would allow direct use of organ level data for parameterization and may provide better predictions. Simple representations of digestion and absorption, splanchnic metabolism, and mammary metabolism of amino acids or protein in aggregate are described. These representations could be used to improve the current system and could serve as a bridge to adoption of more complex models. |
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ISSN: | 0022-0302 1525-3198 |
DOI: | 10.3168/jds.S0022-0302(98)75903-X |