| pubmed-article:2054344 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2054344 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:2054344 | lifeskim:mentions | umls-concept:C0019573 | lld:lifeskim |
| pubmed-article:2054344 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
| pubmed-article:2054344 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:2054344 | pubmed:dateCreated | 1991-8-1 | lld:pubmed |
| pubmed-article:2054344 | pubmed:abstractText | The interaction of hirudin with the dysfunctional enzymes thrombin Quick I and II has been investigated. Natural and recombinant hirudin caused nonlinear competitive inhibition of thrombin Quick I. The results were consistent with thrombin Quick I existing in two forms that have different affinities for hirudin. The affinities of these forms for natural hirudin were respectively 10(4)- and 10(6)-fold lower than that of alpha-thrombin. In contrast, truncated hirudin molecules lacking the C-terminal tail of the molecule caused linear inhibition of thrombin Quick I. These results indicate that different modes of interaction of the two forms of thrombin Quick I with the C-terminal tail of hirudin were the cause of the nonlinear inhibition. Comparison of the dissociation constants of thrombin Quick I with the truncated and full-length forms of hirudin suggested that the interactions that normally occur between the C-terminal tail of hirudin and thrombin were completely disrupted with the low-affinity form of thrombin Quick I. Thrombin Quick II displayed an affinity for natural hirudin that was 10(3)-fold lower than that observed with alpha-thrombin. In contrast, it bound a mutant hirudin with altered N-terminal amino acids only 16-fold less tightly. These results are discussed in terms of structural alterations in the active-site cleft in thrombin Quick II. | lld:pubmed |
| pubmed-article:2054344 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2054344 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2054344 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2054344 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2054344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2054344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2054344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2054344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2054344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2054344 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2054344 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:2054344 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2054344 | pubmed:author | pubmed-author:StoneS RSR | lld:pubmed |
| pubmed-article:2054344 | pubmed:author | pubmed-author:HenriksenR... | lld:pubmed |
| pubmed-article:2054344 | pubmed:author | pubmed-author:SchmitzTT | lld:pubmed |
| pubmed-article:2054344 | pubmed:author | pubmed-author:HofsteengeJJ | lld:pubmed |
| pubmed-article:2054344 | pubmed:author | pubmed-author:DodiAA | lld:pubmed |
| pubmed-article:2054344 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2054344 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:2054344 | pubmed:volume | 30 | lld:pubmed |
| pubmed-article:2054344 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2054344 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2054344 | pubmed:pagination | 6392-7 | lld:pubmed |
| pubmed-article:2054344 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:meshHeading | pubmed-meshheading:2054344-... | lld:pubmed |
| pubmed-article:2054344 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2054344 | pubmed:articleTitle | Interaction of hirudin with the dysthrombins Quick I and II. | lld:pubmed |
| pubmed-article:2054344 | pubmed:affiliation | Friedrich Miescher-Institut, Basel, Switzerland. | lld:pubmed |
| pubmed-article:2054344 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2054344 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2054344 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
