| pubmed-article:8429008 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8429008 | lifeskim:mentions | umls-concept:C0003440 | lld:lifeskim |
| pubmed-article:8429008 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:8429008 | lifeskim:mentions | umls-concept:C0019137 | lld:lifeskim |
| pubmed-article:8429008 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:8429008 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
| pubmed-article:8429008 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8429008 | pubmed:dateCreated | 1993-3-9 | lld:pubmed |
| pubmed-article:8429008 | pubmed:abstractText | Heparin cofactor II and antithrombin are plasma serine proteinase inhibitors whose ability to inhibit alpha-thrombin is accelerated by glycosaminoglycans. Dysfunctional thrombin mutants Quick I (Arg67-->Cys) and Quick II (Gly226-->Val) were used to further compare heparin cofactor II and antithrombin interactions. Quick I, Quick II, and alpha-thrombin were eluted at the same salt concentration from heparin-Sepharose suggesting that the putative heparin-binding site (also termed anion binding exosite-II) is functional. Antithrombin yielded similar inhibition rates for Quick I and alpha-thrombin in the absence or presence of various amounts of heparin. Also, Quick I was inhibited similarly to alpha-thrombin by heparin cofactor II in the absence of glycosaminoglycan. In contrast, glycosaminoglycan-accelerated Quick I inhibition by heparin cofactor II was greatly reduced indicating that anion binding exosite-I (where the mutation occurs in Quick I) is critical for increased inhibition by heparin cofactor II. We also found that heparin cofactor II formed a SDS-resistant bimolecular complex with Quick II and alpha-thrombin at similar rates and the rate of complex formation was accelerated in the presence of glycosaminoglycans. A three-dimensional molecular model of the Quick II active site compared to alpha-thrombin suggested that the heparin cofactor II Leu-Ser-reactive site sequence (P1-P1') is a compatible "pseudosubstrate" in contrast to the Arg-Ser sequence found in antithrombin. The importance of heparin cofactor II as a thrombin regulator will depend upon its ability to interact with glycosaminoglycans and the functional availability of thrombin exosites. | lld:pubmed |
| pubmed-article:8429008 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429008 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429008 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429008 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8429008 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429008 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8429008 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429008 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429008 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429008 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429008 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429008 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8429008 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8429008 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8429008 | pubmed:author | pubmed-author:PhillipsJ EJE | lld:pubmed |
| pubmed-article:8429008 | pubmed:author | pubmed-author:HenriksenR... | lld:pubmed |
| pubmed-article:8429008 | pubmed:author | pubmed-author:ChurchF CFC | lld:pubmed |
| pubmed-article:8429008 | pubmed:author | pubmed-author:WhinnaH CHC | lld:pubmed |
| pubmed-article:8429008 | pubmed:author | pubmed-author:ShirkR ARA | lld:pubmed |
| pubmed-article:8429008 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8429008 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8429008 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8429008 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8429008 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8429008 | pubmed:pagination | 3321-7 | lld:pubmed |
| pubmed-article:8429008 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:meshHeading | pubmed-meshheading:8429008-... | lld:pubmed |
| pubmed-article:8429008 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8429008 | pubmed:articleTitle | Inhibition of dysthrombins Quick I and II by heparin cofactor II and antithrombin. | lld:pubmed |
| pubmed-article:8429008 | pubmed:affiliation | Center for Thrombosis and Hemostasis, University of North Carolina School of Medicine, Chapel Hill 27599-7035. | lld:pubmed |
| pubmed-article:8429008 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8429008 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8429008 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
