pubmed-article:8948492 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8948492 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:8948492 | lifeskim:mentions | umls-concept:C0042878 | lld:lifeskim |
pubmed-article:8948492 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
pubmed-article:8948492 | lifeskim:mentions | umls-concept:C1511572 | lld:lifeskim |
pubmed-article:8948492 | lifeskim:mentions | umls-concept:C0205296 | lld:lifeskim |
pubmed-article:8948492 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:8948492 | pubmed:dateCreated | 1997-1-6 | lld:pubmed |
pubmed-article:8948492 | pubmed:abstractText | Vitamin K belongs to a class of compounds commonly known as prenylquinones. Three other prenylquinones which are abundantly found in food are plastoquinone-9, ubiquinone-9 and ubiquinone-10. Using in vitro assay systems, it was recently found that synthetic derivatives of prenylquinones inhibit the vitamin K-dependent enzyme gamma-glutamylcarboxylase and, to a lesser extent, the vitamin K-epoxide reductase. In this paper we describe how natural prenylquinones affect the vitamin K-dependent enzymes in vitro. All three prenylquinones were found to inhibit both the vitamin K-dependent carboxylase and the K-epoxide reductase in a rat as well as in a cow liver system; 50% inhibition was obtained at concentrations in the micromolar range. On the basis of their respective standard redox potentials, a possible mechanism for the inhibitory effect of prenylquinones on the carboxylase enzyme is put forward. It is concluded that natural prenylquinones are potential antagonists of vitamin K and may interfere with vitamin K-dependent reactions in vivo. | lld:pubmed |
pubmed-article:8948492 | pubmed:language | eng | lld:pubmed |
pubmed-article:8948492 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8948492 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8948492 | pubmed:month | Nov | lld:pubmed |
pubmed-article:8948492 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:8948492 | pubmed:author | pubmed-author:VermeerCC | lld:pubmed |
pubmed-article:8948492 | pubmed:author | pubmed-author:SouteB ABA | lld:pubmed |
pubmed-article:8948492 | pubmed:author | pubmed-author:ThijssenH HHH | lld:pubmed |
pubmed-article:8948492 | pubmed:author | pubmed-author:SaupeJJ | lld:pubmed |
pubmed-article:8948492 | pubmed:author | pubmed-author:RondenJ EJE | lld:pubmed |
pubmed-article:8948492 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8948492 | pubmed:day | 14 | lld:pubmed |
pubmed-article:8948492 | pubmed:volume | 1298 | lld:pubmed |
pubmed-article:8948492 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8948492 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8948492 | pubmed:pagination | 87-94 | lld:pubmed |
pubmed-article:8948492 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:8948492 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8948492 | pubmed:articleTitle | Natural prenylquinones inhibit the enzymes of the vitamin K cycle in vitro. | lld:pubmed |
pubmed-article:8948492 | pubmed:affiliation | Department of Biochemistry, University of Limburg, Maastricht, The Netherlands. | lld:pubmed |
pubmed-article:8948492 | pubmed:publicationType | Journal Article | lld:pubmed |