Document Detail


Metabolism of quercitrin by human intestinal bacteria and its relation to some biological activities.
MedLine Citation:
PMID:  10443478     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
When quercitrin was anaerobically incubated with human intestinal bacteria, quercetin, 3,4-dihydroxyphenylacetic acid and 4-hydroxybenzoic acid were found as metabolites. The main metabolite was quercetin. The bacterium transforming quercitrin to quercetin was Fusobacterium K-60. However, Bacteroides JY-6, which produced alpha-L-rhamnosidase, did not transform quercitrin to quercetin. Among quercitrin and its metabolites, 3,4-dihydroxyphenylacetic acid and 4-hydroxylphenylacetic acid had more potent activity than quercitrin on in vitro anti-platelet aggregation activity, and quercetin and 3,4-dihydroxyphenylacetic acid showed more potent cytotoxicity against tumor cell lines than quercitrin and 4-hydroxylphenylacetic acid.
Authors:
D H Kim; S Y Kim; S Y Park; M J Han
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biological & pharmaceutical bulletin     Volume:  22     ISSN:  0918-6158     ISO Abbreviation:  Biol. Pharm. Bull.     Publication Date:  1999 Jul 
Date Detail:
Created Date:  1999-10-05     Completed Date:  1999-10-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9311984     Medline TA:  Biol Pharm Bull     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  749-51     Citation Subset:  IM    
Affiliation:
College of Pharmacy, Kyung-Hee University, Seoul, Korea.
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MeSH Terms
Descriptor/Qualifier:
Antidiarrheals / metabolism*,  pharmacology
Fusobacterium / drug effects,  metabolism*
Glycoside Hydrolases / metabolism
Humans
Intestines / microbiology*
Platelet Aggregation Inhibitors / pharmacology
Quercetin / analogs & derivatives*,  metabolism,  pharmacology
Chemical
Reg. No./Substance:
0/Antidiarrheals; 0/Platelet Aggregation Inhibitors; 117-39-5/Quercetin; 522-12-3/quercitrin; EC 3.2.1.-/Glycoside Hydrolases; EC 3.2.1.40/alpha-L-rhamnosidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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