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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
1994-6-10
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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=
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chymotrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Leukocyte Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Proteinase Inhibitory Proteins...,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SLPI protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Secretory Leukocyte Peptidase...,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Proteinase Inhibitors
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
33
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5445-50
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7910033-Animals,
pubmed-meshheading:7910033-Cattle,
pubmed-meshheading:7910033-Chymotrypsin,
pubmed-meshheading:7910033-Enzyme Stability,
pubmed-meshheading:7910033-Heparin,
pubmed-meshheading:7910033-Humans,
pubmed-meshheading:7910033-Kinetics,
pubmed-meshheading:7910033-Leukocyte Elastase,
pubmed-meshheading:7910033-Leukocytes,
pubmed-meshheading:7910033-Pancreatic Elastase,
pubmed-meshheading:7910033-Proteinase Inhibitory Proteins, Secretory,
pubmed-meshheading:7910033-Proteins,
pubmed-meshheading:7910033-Secretory Leukocyte Peptidase Inhibitor,
pubmed-meshheading:7910033-Serine Proteinase Inhibitors
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pubmed:year |
1994
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pubmed:articleTitle |
Functions of the N-terminal domain of secretory leukoprotease inhibitor.
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pubmed:affiliation |
Department of Pathology, State University of New York at Stony Brook 11794.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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