| pubmed-article:11420181 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11420181 | lifeskim:mentions | umls-concept:C0007448 | lld:lifeskim |
| pubmed-article:11420181 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:11420181 | lifeskim:mentions | umls-concept:C1706089 | lld:lifeskim |
| pubmed-article:11420181 | lifeskim:mentions | umls-concept:C0968229 | lld:lifeskim |
| pubmed-article:11420181 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:11420181 | pubmed:dateCreated | 2001-6-22 | lld:pubmed |
| pubmed-article:11420181 | pubmed:abstractText | N-Acylethanolamines including anandamide (an endogenous ligand for cannabinoid receptors) are released from N-acylphosphatidylethanolamine (N-acyl-PE) by the catalysis of a phosphodiesterase of the phospholipase D type. The enzyme was solubilized from the particulate fractions of rat heart with the aid of octyl glucoside, and partially purified by anion-exchange chromatography. The enzyme hydrolyzed N-palmitoyl-PE with a specific activity of 17 nmol/min/mg protein at 37 degrees C. The enzyme activity increased dramatically up to 30-fold by millimolar order of Ca(2+). Ca(2+) could be replaced with other divalent cations such as Co(2+), Mg(2+), Mn(2+), Ba(2+), Sr(2+) and Ni(2+). The hydrolysis of N-arachidonoyl-PE (a precursor of anandamide) was also markedly stimulated by Ca(2+). | lld:pubmed |
| pubmed-article:11420181 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11420181 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11420181 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11420181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11420181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11420181 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11420181 | pubmed:month | May | lld:pubmed |
| pubmed-article:11420181 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:11420181 | pubmed:author | pubmed-author:UedaNN | lld:pubmed |
| pubmed-article:11420181 | pubmed:author | pubmed-author:YamanakaKK | lld:pubmed |
| pubmed-article:11420181 | pubmed:author | pubmed-author:LieAA | lld:pubmed |
| pubmed-article:11420181 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11420181 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:11420181 | pubmed:volume | 1532 | lld:pubmed |
| pubmed-article:11420181 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11420181 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11420181 | pubmed:pagination | 121-7 | lld:pubmed |
| pubmed-article:11420181 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:11420181 | pubmed:meshHeading | pubmed-meshheading:11420181... | lld:pubmed |
| pubmed-article:11420181 | pubmed:meshHeading | pubmed-meshheading:11420181... | lld:pubmed |
| pubmed-article:11420181 | pubmed:meshHeading | pubmed-meshheading:11420181... | lld:pubmed |
| pubmed-article:11420181 | pubmed:meshHeading | pubmed-meshheading:11420181... | lld:pubmed |
| pubmed-article:11420181 | pubmed:meshHeading | pubmed-meshheading:11420181... | lld:pubmed |
| pubmed-article:11420181 | pubmed:meshHeading | pubmed-meshheading:11420181... | lld:pubmed |
| pubmed-article:11420181 | pubmed:meshHeading | pubmed-meshheading:11420181... | lld:pubmed |
| pubmed-article:11420181 | pubmed:meshHeading | pubmed-meshheading:11420181... | lld:pubmed |
| pubmed-article:11420181 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11420181 | pubmed:articleTitle | Marked activation of the N-acylphosphatidylethanolamine-hydrolyzing phosphodiesterase by divalent cations. | lld:pubmed |
| pubmed-article:11420181 | pubmed:affiliation | Department of Biochemistry, Tokushima University, School of Medicine, Kuramoto-cho, 770-8503, Tokushima, Japan. nueda@kms.ac.jp | lld:pubmed |
| pubmed-article:11420181 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11420181 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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