| pubmed-article:2446985 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2446985 | lifeskim:mentions | umls-concept:C0040300 | lld:lifeskim |
| pubmed-article:2446985 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:2446985 | lifeskim:mentions | umls-concept:C0019046 | lld:lifeskim |
| pubmed-article:2446985 | lifeskim:mentions | umls-concept:C1880516 | lld:lifeskim |
| pubmed-article:2446985 | lifeskim:mentions | umls-concept:C1285497 | lld:lifeskim |
| pubmed-article:2446985 | lifeskim:mentions | umls-concept:C0597157 | lld:lifeskim |
| pubmed-article:2446985 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:2446985 | lifeskim:mentions | umls-concept:C1550030 | lld:lifeskim |
| pubmed-article:2446985 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:2446985 | pubmed:dateCreated | 1988-2-10 | lld:pubmed |
| pubmed-article:2446985 | pubmed:abstractText | Oxygen affinity of haemoglobin is modulated by several parameters such as the allosteric effector 2-3 DPG for most mammalians. Inositol hexaphosphate (I.H.P.) exerts the same effect on haemoglobin. A previously developed new methodology for the entrapment of drugs into erythrocytes has been adapted to I.H.P.; it is based on a reversible osmotic shock. I.H.P. loaded red blood cells have characteristics very similar to those of native cells. The decrease in oxygen affinity is related to the dose of encapsulated I.H.P. In piglets, transfusion of such cells has led to an increase of oxygen extraction from haemoglobin. Normal anesthetized animals regulate their oxygen consumption by reduction of cardiac output. | lld:pubmed |
| pubmed-article:2446985 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2446985 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2446985 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2446985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2446985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2446985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2446985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2446985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2446985 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2446985 | pubmed:issn | 0323-4347 | lld:pubmed |
| pubmed-article:2446985 | pubmed:author | pubmed-author:TeisseireBB | lld:pubmed |
| pubmed-article:2446985 | pubmed:author | pubmed-author:RoparsCC | lld:pubmed |
| pubmed-article:2446985 | pubmed:author | pubmed-author:NicolauCC | lld:pubmed |
| pubmed-article:2446985 | pubmed:author | pubmed-author:HurelCC | lld:pubmed |
| pubmed-article:2446985 | pubmed:author | pubmed-author:ChassaigneMM | lld:pubmed |
| pubmed-article:2446985 | pubmed:author | pubmed-author:IttiRR | lld:pubmed |
| pubmed-article:2446985 | pubmed:author | pubmed-author:CassejJJ | lld:pubmed |
| pubmed-article:2446985 | pubmed:author | pubmed-author:VillerealM... | lld:pubmed |
| pubmed-article:2446985 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2446985 | pubmed:volume | 114 | lld:pubmed |
| pubmed-article:2446985 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2446985 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2446985 | pubmed:pagination | 488-92 | lld:pubmed |
| pubmed-article:2446985 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:2446985 | pubmed:meshHeading | pubmed-meshheading:2446985-... | lld:pubmed |
| pubmed-article:2446985 | pubmed:meshHeading | pubmed-meshheading:2446985-... | lld:pubmed |
| pubmed-article:2446985 | pubmed:meshHeading | pubmed-meshheading:2446985-... | lld:pubmed |
| pubmed-article:2446985 | pubmed:meshHeading | pubmed-meshheading:2446985-... | lld:pubmed |
| pubmed-article:2446985 | pubmed:meshHeading | pubmed-meshheading:2446985-... | lld:pubmed |
| pubmed-article:2446985 | pubmed:meshHeading | pubmed-meshheading:2446985-... | lld:pubmed |
| pubmed-article:2446985 | pubmed:meshHeading | pubmed-meshheading:2446985-... | lld:pubmed |
| pubmed-article:2446985 | pubmed:meshHeading | pubmed-meshheading:2446985-... | lld:pubmed |
| pubmed-article:2446985 | pubmed:meshHeading | pubmed-meshheading:2446985-... | lld:pubmed |
| pubmed-article:2446985 | pubmed:meshHeading | pubmed-meshheading:2446985-... | lld:pubmed |
| pubmed-article:2446985 | pubmed:meshHeading | pubmed-meshheading:2446985-... | lld:pubmed |
| pubmed-article:2446985 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:2446985 | pubmed:articleTitle | Oxygen transport to tissue modified by entrapment of an allosteric effector of haemoglobin in erythrocytes. | lld:pubmed |
| pubmed-article:2446985 | pubmed:affiliation | Centre National de Transfusion Sanguine, Les Ulis, France. | lld:pubmed |
| pubmed-article:2446985 | pubmed:publicationType | Journal Article | lld:pubmed |
