Journal ArticleDOI
The Systematic Identification of Flavonoids. Von T. J. Mabry, K. R. Markham und M. B. Thomas. 354 S. mit 325 Abb., Springer-Verlag Berlin – Heidelberg – New York 1970, Preis: DM 98, – (US $ 27.00)
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This article is published in Archiv Der Pharmazie.The article was published on 1971-01-01. It has received 371 citations till now.read more
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Analytical separation and detection methods for flavonoids.
Eva de Rijke,Pieter Out,Wilfried M. A. Niessen,Freek Ariese,Cees Gooijer,Udo A. Th. Brinkman +5 more
TL;DR: Special attention will be devoted to the use of tandem-mass spectrometric (MS/MS) techniques for the characterization of several important sub-classes of flavonoids, and to the potential of combined diode-array UV (DAD UV), tandem-MS and nuclear magnetic resonance (NMR) detection for unambiguous identification.
Journal ArticleDOI
Conjugation position of quercetin glucuronides and effect on biological activity
TL;DR: The rate of glucuronidation of quercetin at each position on the polyphenol ring by human liver cell-free extracts containing UDP-glucuronosyltransferases is determined and these compounds can retain some biological activity depending on conjugation position at expected plasma concentrations.
Journal ArticleDOI
Significance of phenolic compounds in plant‐soil‐microbial systems
José Oswaldo Siqueira,Muraleedharan G. Nair,Raymond Hammerschmidt,Gene R. Safir,Alan R. Putnam +4 more
TL;DR: The overall regulation role of these compounds in compatible and incompatible host‐microbe interactions is discussed in this review.
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Interaction of flavonoids with red blood cell membrane lipids and proteins: antioxidant and antihemolytic effects.
TL;DR: It is demonstrated that binding of the flavonoids to the RBC membranes significantly inhibits lipid peroxidation, and at the same time enhances their integrity against hypotonic lysis.
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The interaction of quercetin with human serum albumin: a fluorescence spectroscopic study.
TL;DR: The emission, excitation, and anisotropy data indicate that the quercetin molecules bind at a motionally restricted site near tryptophan-214 in the interdomain cleft region of HSA, and the excitation spectrum suggests occurrence of efficient Förster type resonance energy transfer (FRET) from the single tryptophile residue of H SA to the protein bound quercETin.