| pubmed-article:2920011 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2920011 | lifeskim:mentions | umls-concept:C0019134 | lld:lifeskim |
| pubmed-article:2920011 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:2920011 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:2920011 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2920011 | pubmed:dateCreated | 1989-4-6 | lld:pubmed |
| pubmed-article:2920011 | pubmed:abstractText | In order to determine the specificity of the interaction between thrombin and glia-derived nexin (GdN), the inactivation of proteolytically modified human thrombin species by GdN has been studied. The second-order rate constants for the inactivation of alpha-, beta T-, gamma T- and epsilon-thrombin by GdN were 1.41, 0.63, 0.33 and 1.91 microM-1.s-1 respectively. The kinetic properties of gdN were also investigated in the presence of different types of heparin, fractionated according to antithrombin III-binding affinity. Association rate constants of both gdN and antithrombin III with alpha-thrombin were obtained using unfractionated, low- and high-affinity heparin types. The different heparin types gave optimal rates of inhibition at similar heparin concentrations for both inhibitors. At optimal heparin concentrations, the rate of inactivation of alpha-thrombin by GdN was 0.5-1.2 nM-1.s-1, which suggests that, under these conditions, the interaction is diffusion-controlled. | lld:pubmed |
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| pubmed-article:2920011 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2920011 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2920011 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2920011 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2920011 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:2920011 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2920011 | pubmed:author | pubmed-author:WallaceAA | lld:pubmed |
| pubmed-article:2920011 | pubmed:author | pubmed-author:StoneS RSR | lld:pubmed |
| pubmed-article:2920011 | pubmed:author | pubmed-author:HofsteengeJJ | lld:pubmed |
| pubmed-article:2920011 | pubmed:author | pubmed-author:RovelliGG | lld:pubmed |
| pubmed-article:2920011 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2920011 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2920011 | pubmed:volume | 257 | lld:pubmed |
| pubmed-article:2920011 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2920011 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2920011 | pubmed:pagination | 191-6 | lld:pubmed |
| pubmed-article:2920011 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:2920011 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2920011 | pubmed:articleTitle | Effect of heparin on the glia-derived-nexin-thrombin interaction. | lld:pubmed |
| pubmed-article:2920011 | pubmed:affiliation | Friedrich Miescher-Institut, Basel, Switzerland. | lld:pubmed |
| pubmed-article:2920011 | pubmed:publicationType | Journal Article | lld:pubmed |
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