| pubmed-article:7929416 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7929416 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7929416 | lifeskim:mentions | umls-concept:C0005778 | lld:lifeskim |
| pubmed-article:7929416 | lifeskim:mentions | umls-concept:C0205102 | lld:lifeskim |
| pubmed-article:7929416 | lifeskim:mentions | umls-concept:C0019134 | lld:lifeskim |
| pubmed-article:7929416 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:7929416 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:7929416 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:7929416 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:7929416 | lifeskim:mentions | umls-concept:C0054578 | lld:lifeskim |
| pubmed-article:7929416 | pubmed:issue | 43 | lld:pubmed |
| pubmed-article:7929416 | pubmed:dateCreated | 1994-11-23 | lld:pubmed |
| pubmed-article:7929416 | pubmed:abstractText | The effect of heparin and other glycosaminoglycans on the activation of factor X by the phospholipid membrane-bound human factor IXa-factor VIIIa complex (intrinsic fXase) was studied. Standard heparin inhibited purified intrinsic fXase by 50% at approximately 0.08 unit/ml (0.4 microgram/ml), which is below the normal range of heparin concentrations achieved during antithrombotic therapy (0.2-0.7 unit/ml). Kinetic and binding experiments revealed that heparin behaves as a partial noncompetitive inhibitor. The inhibition constant of heparin with low affinity for antithrombin was indistinguishable from heparin with high affinity for antithrombin (Ki = 20 nM). Additionally, "low molecular weight" heparin, which also is used as an antithrombotic drug, was a potent inhibitor of intrinsic fXase (Ki = 60 nM). Dermatan sulfate inhibited intrinsic fXase much more weakly than standard heparin (IC50 = 80 micrograms/ml). The IC50 of the other mammalian glycosaminoglycans, chondroitin sulfate, keratan sulfate, and hyaluronic acid, were greater than 100 micrograms/ml. Purified prothrombinase and extrinsic fXase were not inhibited by heparin. We propose that part of the antithrombotic action of heparin and low molecular weight heparin is due to anti-thrombin-independent inhibition of intrinsic fXase and that heparin with low affinity for antithrombin may be useful as an antithrombotic agent. | lld:pubmed |
| pubmed-article:7929416 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7929416 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7929416 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7929416 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7929416 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7929416 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7929416 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7929416 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7929416 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7929416 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7929416 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7929416 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7929416 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7929416 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7929416 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:7929416 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7929416 | pubmed:author | pubmed-author:ParkerE TET | lld:pubmed |
| pubmed-article:7929416 | pubmed:author | pubmed-author:LollarPP | lld:pubmed |
| pubmed-article:7929416 | pubmed:author | pubmed-author:KrishnaswamyS... | lld:pubmed |
| pubmed-article:7929416 | pubmed:author | pubmed-author:BarrowR TRT | lld:pubmed |
| pubmed-article:7929416 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7929416 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:7929416 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:7929416 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7929416 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7929416 | pubmed:pagination | 26796-800 | lld:pubmed |
| pubmed-article:7929416 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7929416 | pubmed:meshHeading | pubmed-meshheading:7929416-... | lld:pubmed |
| pubmed-article:7929416 | pubmed:meshHeading | pubmed-meshheading:7929416-... | lld:pubmed |
| pubmed-article:7929416 | pubmed:meshHeading | pubmed-meshheading:7929416-... | lld:pubmed |
| pubmed-article:7929416 | pubmed:meshHeading | pubmed-meshheading:7929416-... | lld:pubmed |
| pubmed-article:7929416 | pubmed:meshHeading | pubmed-meshheading:7929416-... | lld:pubmed |
| pubmed-article:7929416 | pubmed:meshHeading | pubmed-meshheading:7929416-... | lld:pubmed |
| pubmed-article:7929416 | pubmed:meshHeading | pubmed-meshheading:7929416-... | lld:pubmed |
| pubmed-article:7929416 | pubmed:meshHeading | pubmed-meshheading:7929416-... | lld:pubmed |
| pubmed-article:7929416 | pubmed:meshHeading | pubmed-meshheading:7929416-... | lld:pubmed |
| pubmed-article:7929416 | pubmed:meshHeading | pubmed-meshheading:7929416-... | lld:pubmed |
| pubmed-article:7929416 | pubmed:meshHeading | pubmed-meshheading:7929416-... | lld:pubmed |
| pubmed-article:7929416 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7929416 | pubmed:articleTitle | Inhibition by heparin of the human blood coagulation intrinsic pathway factor X activator. | lld:pubmed |
| pubmed-article:7929416 | pubmed:affiliation | Department of Medicine, Emory University, Atlanta, Georgia 30322. | lld:pubmed |
| pubmed-article:7929416 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7929416 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7929416 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7929416 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7929416 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7929416 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7929416 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7929416 | lld:pubmed |
