| pubmed-article:8865821 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8865821 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8865821 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:8865821 | lifeskim:mentions | umls-concept:C0855173 | lld:lifeskim |
| pubmed-article:8865821 | lifeskim:mentions | umls-concept:C1159794 | lld:lifeskim |
| pubmed-article:8865821 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8865821 | pubmed:dateCreated | 1996-11-19 | lld:pubmed |
| pubmed-article:8865821 | pubmed:abstractText | The JAR human placental choriocarcinoma cells were found to transport carnitine into the intracellular space by a Na(+)-dependent process. The transport showed no requirement for anions. The Na+-dependent process was saturable and the apparent Michaelis-Menten constant for carnitine was 12.3 +/- 0.5 microM. Na+ activated the transport by increasing the affinity of the transport system for carnitine. The transport system specifically interacted with L-carnitine, D-carnitine, acetyl-DL-carnitine and betaine. 6-N-Trimethyllysine and choline had little or no effect on carnitine transport. Of the total transport measured, transport into the intracellular space represented 90%. Plasma membrane vesicles prepared from JAR cells were found to bind carnitine in a Na(+)-dependent manner. The binding was saturable with an apparent dissociation constant of 0.66 +/- 0.08 microM. The binding process was specific for L-carnitine, D-carnitine, acetyl-DL-carnitine, and betaine. 6-N-Trimethyllysine and choline showed little or no affinity. It is concluded that the JAR cells express a Na(+)-dependent high-affinity system for carnitine transport and that the Na(+)-dependent high-affinity carnitine binding detected in purified JAR cell plasma membrane vesicles is possibly related to the transmembrane transport process. | lld:pubmed |
| pubmed-article:8865821 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8865821 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8865821 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8865821 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8865821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8865821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8865821 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8865821 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8865821 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:8865821 | pubmed:author | pubmed-author:LeibachF HFH | lld:pubmed |
| pubmed-article:8865821 | pubmed:author | pubmed-author:HuangWW | lld:pubmed |
| pubmed-article:8865821 | pubmed:author | pubmed-author:RamamoorthySS | lld:pubmed |
| pubmed-article:8865821 | pubmed:author | pubmed-author:GanapathyVV | lld:pubmed |
| pubmed-article:8865821 | pubmed:author | pubmed-author:CarterA LAL | lld:pubmed |
| pubmed-article:8865821 | pubmed:author | pubmed-author:PrasadP DPD | lld:pubmed |
| pubmed-article:8865821 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8865821 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:8865821 | pubmed:volume | 1284 | lld:pubmed |
| pubmed-article:8865821 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8865821 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8865821 | pubmed:pagination | 109-17 | lld:pubmed |
| pubmed-article:8865821 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:meshHeading | pubmed-meshheading:8865821-... | lld:pubmed |
| pubmed-article:8865821 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8865821 | pubmed:articleTitle | Sodium-dependent carnitine transport in human placental choriocarcinoma cells. | lld:pubmed |
| pubmed-article:8865821 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta 30912-2100, USA. | lld:pubmed |
| pubmed-article:8865821 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8865821 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8865821 | lld:pubmed |
