| pubmed-article:7910033 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7910033 | lifeskim:mentions | umls-concept:C0052059 | lld:lifeskim |
| pubmed-article:7910033 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:7910033 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7910033 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:7910033 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:7910033 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:7910033 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:7910033 | pubmed:dateCreated | 1994-6-10 | lld:pubmed |
| pubmed-article:7910033 | pubmed:abstractText | Secretory leukoprotease inhibitor (SLPI) comprises two homologous domains: the C-terminal domain contains the reactive site, while the function of the N-terminal domain remains unknown. In order to elucidate the function of the N-terminal domain, we studied the kinetics of reactions of human leukocyte elastase with two recombinant forms of SLPI: the full-length inhibitor and the C-terminal domain alone. The reactions of elastase with the full-length inhibitor and the C-terminal domain share the same association rate constant, 2 x 10(6) M-1 s-1, but the complex formed with the C-terminal domain is less stable, with a dissociation rate constant of 8 x 10(-4) s-1, 5 times higher than that of the complex with the full-length inhibitor. The binding of the full-length inhibitor to elastase is greatly accelerated by polyanions. In the presence of submicromolar concentrations (1 microgram/mL) of heparin, the association rate constant is increased by more than 1 order of magnitude. The binding of the C-terminal domain alone to elastase shows much lower sensitivity to heparin; in the presence of 5 microM (25 micrograms/mL) heparin, association of the C-terminal domain with elastase reaches a maximum rate of 7 x 10(6) M-1 s-1, about 3 times higher than the rate in the absence of heparin. Similar differential effects of heparin have been observed on the reactions of alpha-chymotrypsin with the two recombinant forms of SLPI.2= | lld:pubmed |
| pubmed-article:7910033 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7910033 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7910033 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7910033 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7910033 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7910033 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7910033 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7910033 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7910033 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7910033 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7910033 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7910033 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7910033 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7910033 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7910033 | pubmed:month | May | lld:pubmed |
| pubmed-article:7910033 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:7910033 | pubmed:author | pubmed-author:SimonS RSR | lld:pubmed |
| pubmed-article:7910033 | pubmed:author | pubmed-author:KemmeMM | lld:pubmed |
| pubmed-article:7910033 | pubmed:author | pubmed-author:YingQ LQL | lld:pubmed |
| pubmed-article:7910033 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7910033 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:7910033 | pubmed:volume | 33 | lld:pubmed |
| pubmed-article:7910033 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7910033 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7910033 | pubmed:pagination | 5445-50 | lld:pubmed |
| pubmed-article:7910033 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7910033 | pubmed:meshHeading | pubmed-meshheading:7910033-... | lld:pubmed |
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| pubmed-article:7910033 | pubmed:meshHeading | pubmed-meshheading:7910033-... | lld:pubmed |
| pubmed-article:7910033 | pubmed:meshHeading | pubmed-meshheading:7910033-... | lld:pubmed |
| pubmed-article:7910033 | pubmed:meshHeading | pubmed-meshheading:7910033-... | lld:pubmed |
| pubmed-article:7910033 | pubmed:meshHeading | pubmed-meshheading:7910033-... | lld:pubmed |
| pubmed-article:7910033 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7910033 | pubmed:articleTitle | Functions of the N-terminal domain of secretory leukoprotease inhibitor. | lld:pubmed |
| pubmed-article:7910033 | pubmed:affiliation | Department of Pathology, State University of New York at Stony Brook 11794. | lld:pubmed |
| pubmed-article:7910033 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7910033 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7910033 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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