Source:http://linkedlifedata.com/resource/pubmed/id/12162571
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2002-8-6
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pubmed:abstractText |
Transglutaminases catalyze the cross-linking and amine incorporation of proteins, and are implicated in various biological phenomena. Previously, we found a high molecular mass transglutaminase-inhibitory substance produced by Streptomyces lavendulae Y-200 that appeared to be a melanin substance. Here, we report that synthetic tyrosine melanin inhibited various types of transglutaminases. Tyrosine melanin inhibited tissue-type transglutaminase in a competitive manner with a glutamine substrate, and also inhibited the cross-linking of casein catalyzed by a tissue-type transglutaminase. The melanized hemolymph of the silkworm and melanin solutions prepared from melanin precursors inhibited tissue-type transglutaminase. These results suggested that the melanin substances generally inhibit transglutaminases.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0916-8451
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1412-4
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:12162571-Animals,
pubmed-meshheading:12162571-Bombyx,
pubmed-meshheading:12162571-Caseins,
pubmed-meshheading:12162571-Dose-Response Relationship, Drug,
pubmed-meshheading:12162571-Guinea Pigs,
pubmed-meshheading:12162571-Liver,
pubmed-meshheading:12162571-Melanins,
pubmed-meshheading:12162571-Transglutaminases,
pubmed-meshheading:12162571-Tyrosine
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pubmed:year |
2002
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pubmed:articleTitle |
Inhibition of transglutaminase by synthetic tyrosine melanin.
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pubmed:affiliation |
Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Japan. ikura@ipc.kit.ac.jp
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pubmed:publicationType |
Journal Article
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