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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
1995-4-10
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pubmed:abstractText |
Cupressus sempervirens L. proanthocyanidolic (O.P.C.) oligomers inhibited the esterolytic activity of pancreatic elastase with a Cl50 of 0.0075 mg/ml when a sap substrate suc(Al)3NA was used in a Tris-HCl 0.05 M buffer with a pH of 7.5. Inhibition was slightly lower when the ionic strength of the buffer was increased. Elastolytic activity was inhibited using an elastinorcein substrate with a Cl50 of 0.05 mg/ml, whatever the pH or the ionic strength of the buffer. The oligomers bound with the elastase to form a precipitant complex where a 2 mg/ml concentration of oligomers precipitated the elastase at 1 mg/ml. Insoluble elastin fixed few 150 micrograms oligomers for 1 mg of elastin but the latter was partly protected by the subsequent action of the elastase. Soluble elastin fixed a greater number of oligomers but it was the peptids of elastin enzyme hydrolysis which fixed the largest amount: around 1500 micrograms per mg. The oligomers-elastin complex seems to be more stable than that of oligomers-elastase which regains part of its esterase activity. The elastic fibers seem to be protected by the O.P.C.
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pubmed:language |
fre
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0047-2166
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
49
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
453-61
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:articleTitle |
[The interaction of Cupressus sempervirens L. proanthocyanidolic oligomers with elastase and elastins].
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pubmed:affiliation |
Laboratoire de Pharmacologie et de Pharmacie Clinique, Faculté de Pharmacie, Clermont-Ferrant, France.
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pubmed:publicationType |
Journal Article,
English Abstract
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