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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1985-7-11
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pubmed:abstractText |
12-L-hydroxy-5,8,10-heptadecatrienoic acid (HHT) was found to be an excellent substrate for NAD+ dependent 15-hydroxyprostaglandin dehydrogenase from porcine kidney. Kcat/Km value of HHT was comparable to that of prostaglandin E although HHT is not a prostanoic acid derivative. Product of enzyme catalyzed oxidation of HHT was identified as 12-keto-5,8,10-heptadecatrienoic acid by gas chromatography-mass spectrometry. The fact that HHT is an excellent substrate for 15-hydroxyprostaglandin dehydrogenase suggest that HHT may have profound unrecognized biological actions and its inactivation may be via oxidation of the hydroxyl group.
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pubmed:grant |
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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 |
May
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
129
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
268-74
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:4004878-Animals,
pubmed-meshheading:4004878-Chromatography, Thin Layer,
pubmed-meshheading:4004878-Fatty Acids, Unsaturated,
pubmed-meshheading:4004878-Gas Chromatography-Mass Spectrometry,
pubmed-meshheading:4004878-Hydroxyprostaglandin Dehydrogenases,
pubmed-meshheading:4004878-Kidney,
pubmed-meshheading:4004878-Kinetics,
pubmed-meshheading:4004878-NAD,
pubmed-meshheading:4004878-Spectrometry, Fluorescence,
pubmed-meshheading:4004878-Swine
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pubmed:year |
1985
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pubmed:articleTitle |
12-L-hydroxy-5,8,10-heptadecatrienoic acid (HHT) is an excellent substrate for NAD+-dependent 15-hydroxyprostaglandin dehydrogenase.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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