| Nutritional requirements of Allisonella histaminiformans, a ruminal bacterium that decarboxylates histidine and produces histamine. | |
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MedLine Citation:
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PMID: 15386119 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Histamine is an inflammatory agent that contributes to bovine laminitis. Cattle fed silage-containing rations often have large populations of Allisonella histaminiformans, but this obligate histidine-decarboxylating bacterium could not be isolated from cattle fed timothy hay. The growth of A. histaminiformans was stimulated by yeast extract, protein hydrolysates, and water-soluble extracts of alfalfa or corn silage. Extracts of alfalfa were more potent than corn silage. Because growth and histamine production were not stimulated by Casamino Acids or a mixture of purified amino acids, it appeared that A. histaminiformans requires peptides. The idea that A. histaminiformans requires peptides is consistent with the observation that alfalfa silages often have a large amount of peptide nitrogen. |
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Authors:
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Matthew R Garner; Matthew R Gronquist; James B Russell |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Current microbiology Volume: 49 ISSN: 0343-8651 ISO Abbreviation: Curr. Microbiol. Publication Date: 2004 Oct |
Date Detail:
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Created Date: 2004-09-23 Completed Date: 2004-11-04 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7808448 Medline TA: Curr Microbiol Country: United States |
Other Details:
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Languages: eng Pagination: 295-9 Citation Subset: IM |
Affiliation:
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Department of Microbiology, Cornell University, Ithaca, NY 14853, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acidaminococcaceae
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enzymology,
metabolism* Animal Feed / microbiology Animals Cattle Culture Media Histamine / biosynthesis* Histidine / metabolism* Histidine Decarboxylase / metabolism* Medicago sativa / metabolism Rumen / microbiology* Silage / microbiology* Zea mays / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Culture Media; 51-45-6/Histamine; 71-00-1/Histidine; EC 4.1.1.22/Histidine Decarboxylase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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