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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1990-12-6
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pubmed:abstractText |
Recombinant eglin c is a potent reversible inhibitor of human pancreatic elastase. At pH 7.4 and 25 degrees C, kass. = 7.3 x 10(5) M-1.s-1, kdiss. = 2.7 x 10(-4) s-1 and Ki = 3.7 x 10(-10) M. Stopped-flow kinetic indicate that the formation of the stable enzyme-inhibitor complex is not preceded by a fast pre-equilibrium complex or that the latter has a dissociation constant greater than 0.3 microM. The elastase-eglin c complex is much less stable at pH 5.0 and 25 degrees C, where kdiss. = 1.1 x 10(-2) s-1 and Ki = 7.3 x 10(-8) M. At pH 7.4 the activation energy for kass. is 43.9 kJ.mol-1 (10.5 kcal.mol-1). The kass. increases between pH 5.0 and 8.0 and remains essentially constant up to pH 9.0. This pH-dependence could not be described by a simple ionization curve. Both alpha 2-macroglobulin and alpha 1-proteinase inhibitor are able to dissociate the elastase-eglin c complex, as evidenced by measurement of the enzymic activity of alpha 2-macroglobulin-bound elastase or by polyacrylamide-gel electrophoresis of mixtures of alpha 1-proteinase inhibitor and elastase-eglin c complex. The rough estimate of kdiss. obtained with the alpha 2-macroglobulin dissociation experiment (1.6 x 10(-4) s-1) was of the same order of magnitude as the constant measured with the progress curve method. Eglin c strongly inhibits the solubilization of human aorta elastin by human pancreatic elastase. The extent of inhibition is the same whether elastase is added to a suspension of elastin and eglin c or whether elastase is preincubated with elastin for 3 min before addition of eglin c. However, the efficiency of the inhibitor sharply decreases if elastase is reacted with elastin for more prolonged periods.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-1212266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-14321178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-2465784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-2471515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-3301348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-3427074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-3492198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-3530282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-3644643,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-3649242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-3843961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-4857588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6139913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6153274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6153632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6204977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6382168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6517881,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6562888,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6609797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6847616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6898442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6912862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6918355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-6996568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-819031,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-924384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1700695-92900
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
639-44
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1700695-Elastin,
pubmed-meshheading:1700695-Humans,
pubmed-meshheading:1700695-Hydrogen-Ion Concentration,
pubmed-meshheading:1700695-Kinetics,
pubmed-meshheading:1700695-Pancreas,
pubmed-meshheading:1700695-Pancreatic Elastase,
pubmed-meshheading:1700695-Proteins,
pubmed-meshheading:1700695-Recombinant Proteins,
pubmed-meshheading:1700695-Serine Proteinase Inhibitors,
pubmed-meshheading:1700695-Serpins,
pubmed-meshheading:1700695-Temperature,
pubmed-meshheading:1700695-alpha 1-Antitrypsin,
pubmed-meshheading:1700695-alpha-Macroglobulins
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pubmed:year |
1990
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pubmed:articleTitle |
Kinetics of the inhibition of human pancreatic elastase by recombinant eglin c. Influence of elastin.
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pubmed:affiliation |
I.N.S.E.R.M. Unité 237, Faculté de Pharmacie, Université Louis Pasteur de Strasbourg, Illkirch, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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