| pubmed-article:6466692 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6466692 | lifeskim:mentions | umls-concept:C0012984 | lld:lifeskim |
| pubmed-article:6466692 | lifeskim:mentions | umls-concept:C1522564 | lld:lifeskim |
| pubmed-article:6466692 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:6466692 | lifeskim:mentions | umls-concept:C0070789 | lld:lifeskim |
| pubmed-article:6466692 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6466692 | pubmed:dateCreated | 1984-10-3 | lld:pubmed |
| pubmed-article:6466692 | pubmed:abstractText | Dog heart contains a membrane bound N-acyltransferase (transacylase) which transfers acyl groups from the sn-1 position of membrane phospholipids to the amino group of ethanolamine phospholipids in the presence of millimolar Ca2+ concentrations. Using crude membrane preparations, we found this N-acyltransferase activity to be heat sensitive and inhibited by sulfhydryl reagents. Pretreatment of a membrane fraction with trypsin reduced N-acyltransferase activity to 60% while pretreatment with trypsin and Triton X-100 together reduced it to 30% of the control value. At pH 8.0 both Sr2+ and Mn2+ could fully substitute for Ca2+ with respect to optimum ion concentration and molecular species of the product formed in dog heart membranes from endogenous substrates. Ba2+ was equally effective in achieving N-acylation of ethanolamine phospholipids while other divalent cations were less effective or ineffective. The reaction exhibited a pH optimum of 8.5 to 9.0 with both Ca2+ and Sr2+ while Mn2+ precipitated above pH 8.0 resulting in decreased N-acylation activity. Both phosphatidylcholine and 1-acyl lysophosphatidylcholine could serve as acyl donors. Triton X-100 at a concentration of 0.1% stimulated acyl transfer from exogenous phosphatidylcholine but inhibited acyl transfer from lysophosphatidylcholine. | lld:pubmed |
| pubmed-article:6466692 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6466692 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6466692 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6466692 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6466692 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6466692 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6466692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6466692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6466692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6466692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6466692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6466692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6466692 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6466692 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:6466692 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:6466692 | pubmed:author | pubmed-author:MuramatsuTT | lld:pubmed |
| pubmed-article:6466692 | pubmed:author | pubmed-author:SchmidP CPC | lld:pubmed |
| pubmed-article:6466692 | pubmed:author | pubmed-author:ReddyP VPV | lld:pubmed |
| pubmed-article:6466692 | pubmed:author | pubmed-author:SchmidH HHH | lld:pubmed |
| pubmed-article:6466692 | pubmed:author | pubmed-author:NatarajanVV | lld:pubmed |
| pubmed-article:6466692 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6466692 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:6466692 | pubmed:volume | 795 | lld:pubmed |
| pubmed-article:6466692 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6466692 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6466692 | pubmed:pagination | 130-6 | lld:pubmed |
| pubmed-article:6466692 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:6466692 | pubmed:meshHeading | pubmed-meshheading:6466692-... | lld:pubmed |
| pubmed-article:6466692 | pubmed:meshHeading | pubmed-meshheading:6466692-... | lld:pubmed |
| pubmed-article:6466692 | pubmed:meshHeading | pubmed-meshheading:6466692-... | lld:pubmed |
| pubmed-article:6466692 | pubmed:meshHeading | pubmed-meshheading:6466692-... | lld:pubmed |
| pubmed-article:6466692 | pubmed:meshHeading | pubmed-meshheading:6466692-... | lld:pubmed |
| pubmed-article:6466692 | pubmed:meshHeading | pubmed-meshheading:6466692-... | lld:pubmed |
| pubmed-article:6466692 | pubmed:meshHeading | pubmed-meshheading:6466692-... | lld:pubmed |
| pubmed-article:6466692 | pubmed:meshHeading | pubmed-meshheading:6466692-... | lld:pubmed |
| pubmed-article:6466692 | pubmed:meshHeading | pubmed-meshheading:6466692-... | lld:pubmed |
| pubmed-article:6466692 | pubmed:meshHeading | pubmed-meshheading:6466692-... | lld:pubmed |
| pubmed-article:6466692 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6466692 | pubmed:articleTitle | Properties of canine myocardial phosphatidylethanolamine N-acyltransferase. | lld:pubmed |
| pubmed-article:6466692 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6466692 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6466692 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6466692 | lld:pubmed |
