| Methionine metabolism in piglets Fed DL-methionine or its hydroxy analogue was affected by distribution of enzymes oxidizing these sources to keto-methionine. | |
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MedLine Citation:
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PMID: 20073466 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Previous evidence shows that the extensive catabolism of dietary essential amino acids (AA) by the intestine results in decreased availability of these AA for protein synthesis in extraintestinal tissues. This raises the possibility that extraintestinal availability of AA may be improved by supplying the animal with an AA source more of which can bypass the intestine. To test this hypothesis, six barrows (35-day-old, 8.6 +/- 1.4 kg), implanted with arterial, portal, and mesenteric catheters, were fed a DL-methionine (DL-MET) or DL-2-hydroxy-4-methylthiobutyrate (DL-HMTB) diet once hourly and infused intramesenterically with 1% p-amino hippurate. Although the directly available L-MET in DL-MET diet was about 1.2-fold that in DL-HMTB diet, the net portal appearance of L-MET was not different between the two diets. Compared with the low mRNA abundance and low activity of D-2-hydroxy acid dehydrogenase (D-HADH) and l-2-hydroxy acid oxidase (L-HAOX) in the intestine, the high mRNA abundance and high activity of D-AA oxidase (D-AAOX) indicated that the intestine had a relatively higher capacity of D-MET utilization than of dl-HMTB utilization to L-MET synthesis and its subsequent metabolism. However, in contrast to the much lower D-AAOX activity (nmol/g tissue) in the stomach than in the liver and kidney, both d-HADH and L-HAOX activity in the stomach was comparable with those in the liver and/or kidney, indicating the substantial capacity of the stomach to convert DL-HMTB to L-MET. Collectively, the difference in distribution of activity and mRNA abundance of D-AAOX, D-HADH, and L-HAOX in the piglets may offer a biological basis for the similar portal appearance of L-MET between DL-MET and DL-HMTB diets, and thus may provide new important insights into nutritional efficiency of different L-MET sources. |
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Authors:
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Zhengfeng Fang; Hefeng Luo; Hongkui Wei; Feiruo Huang; Zhili Qi; Siwen Jiang; Jian Peng |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of agricultural and food chemistry Volume: 58 ISSN: 1520-5118 ISO Abbreviation: J. Agric. Food Chem. Publication Date: 2010 Feb |
Date Detail:
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Created Date: 2010-02-03 Completed Date: 2010-04-19 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0374755 Medline TA: J Agric Food Chem Country: United States |
Other Details:
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Languages: eng Pagination: 2008-14 Citation Subset: IM |
Affiliation:
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Key Lab of Animal Genetics, Breeding and Reproduction of Ministry of Education & Key Lab of Swine Genetics and Breeding of Ministry of Agriculture, Department of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agricultural University, Wuhan 430070, PR China. |
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| MeSH Terms | |
Descriptor/Qualifier:
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Alcohol Oxidoreductases
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genetics,
metabolism* Amidohydrolases / genetics, metabolism* Animal Feed / analysis* Animal Nutritional Physiological Phenomena Animals Female Intestines / enzymology, metabolism Male Methionine / analogs & derivatives, metabolism* Oxidation-Reduction Stomach / enzymology, metabolism Swine / metabolism* |
| Chemical | |
Reg. No./Substance:
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63-68-3/Methionine; EC 1.1.-/Alcohol Oxidoreductases; EC 1.1.3.15/L-2-hydroxyacid oxidase; EC 1.1.99.6/D-2-hydroxyacid dehydrogenase; EC 3.5.-/Amidohydrolases; EC 3.5.1.-/N-acyl-D-aspartate amidohydrolase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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