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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1993-2-5
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pubmed:abstractText |
A protease from house dust mite(Dermatophagoides farinae) having high specificity towards a substrate of blood coagulation factor XIIa catalyzes the activation of kallikrein-kinin system in plasma (Takahashi et al., 1990). To prevent the formation of kinin by the mite-protease, inhibition of the protease with its inhibitors was tested in vitro and in vivo. Its kinetic studies revealed that Ki values are 3.9 x 10(-10) M for aprotinin, 3.0 x 10(-9) M for soybean trypsin inhibitor (Kunitz) and 2.5 x 10(-8) M for gabexate mesylate. Enhancement of blood permeability in guinea pigs caused by the protease was markedly suppressed by these inhibitors.
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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 |
Dec
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pubmed:issn |
0158-5231
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
717-23
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:1282814-Animals,
pubmed-meshheading:1282814-Aprotinin,
pubmed-meshheading:1282814-Binding, Competitive,
pubmed-meshheading:1282814-Capillary Permeability,
pubmed-meshheading:1282814-Endopeptidases,
pubmed-meshheading:1282814-Factor XIIa,
pubmed-meshheading:1282814-Gabexate,
pubmed-meshheading:1282814-Guinea Pigs,
pubmed-meshheading:1282814-Kallikrein-Kinin System,
pubmed-meshheading:1282814-Kallikreins,
pubmed-meshheading:1282814-Kinetics,
pubmed-meshheading:1282814-Mites,
pubmed-meshheading:1282814-Protease Inhibitors,
pubmed-meshheading:1282814-Skin,
pubmed-meshheading:1282814-Substrate Specificity,
pubmed-meshheading:1282814-Trypsin Inhibitor, Kunitz Soybean
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pubmed:year |
1992
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pubmed:articleTitle |
Inhibition of mite protease (Df-protease) with protease inhibitors.
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pubmed:affiliation |
Department of Materials Science, Toin University, Yokohama, Japan.
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pubmed:publicationType |
Journal Article
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