tannins and eugeniin

tannins has been researched along with eugeniin* in 3 studies

Other Studies

3 other study(ies) available for tannins and eugeniin

ArticleYear
Biochemical characterization of galloyl pedunculagin (ellagitannin) as a selective inhibitor of the beta-regulatory subunit of A-kinase in vitro.
    Journal of biochemistry, 2001, Volume: 129, Issue:3

    The inhibitory effects of galloyl pedunculagin (GP) and eugeniin on the phosphorylation of histone H2B by cAMP-dependent protein kinase (A-kinase) and autophosphorylation of its beta-regulatory subunit (A-kinase beta) were examined in vitro. It was found that (i) GP (ID(50) = approx. 50 nM) effectively inhibits the activity of A-kinase (heterodimer), but high doses are required to inhibit the activities of the alpha-catalytic subunit (ID(50) = approx. 0.25 microM) and casein kinase II (CK-II, ID(50) = approx. 0.6 microM); (ii) GP inhibits the autophosphorylation of A-kinase beta in a dose-dependent manner with an ID(50) of approx. 6.6 nM, which is about 30-fold lower than that observed with CK-II beta; and (iii) GP reduces the suppressive effect of the beta-subunit on the activity of the alpha-subunit. In addition, purified bovine heart A-kinase precipitates when incubated with excess GP at pH 5.0. A similar precipitation of A-kinase was observed with eugeniin. These results show that the direct binding of GP to the beta-subunit prevents the physiological interaction between the beta- and alpha-subunits of A-kinase in vitro. This conclusion is presumably consistent with the binding affinity of proline-rich proteins with tannins, since A-kinase beta contains a proline-rich domain that interacts with GP or eugeniin. Therefore, GP will serve as a powerful inhibitor for in vitro and in vivo cellular studies of A-kinase beta-mediated signal transduction.

    Topics: Animals; Antioxidants; Binding Sites; Casein Kinase II; Catalytic Domain; Cattle; Chemical Precipitation; Cyclic AMP-Dependent Protein Kinases; Dimerization; Dose-Response Relationship, Drug; Enzyme Inhibitors; Flavonoids; Gallic Acid; Glucosides; Histones; Hydrolyzable Tannins; Kinetics; Molecular Structure; Phenols; Phosphorylation; Polymers; Protein Binding; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Protein Subunits; Quercetin; Substrate Specificity; Swine; Tannins

2001
Inhibitory effects of ellagi- and gallotannins on rat intestinal alpha-glucosidase complexes.
    Bioscience, biotechnology, and biochemistry, 2001, Volume: 65, Issue:3

    The clove ellagitannins and their related polygalloyl-glucoses inhibited maltase activity of rat intestinal alpha-glucosidases. The structure-activity relationship study of those galloylglucoses, varying the extent of galloylation on the glucose core, with the ellagitannins, indicated that an increasing number of galloyl units in the molecule lead to an increase in the inhibitory activity. Penta-O-galloyl-beta-D-glucose, with five galloyl groups showed the highest inhibitory activity. On the other hand, hexahydroxydiphenoyl units contained in the ellagitannins had little effect on the activity. After separation of maltase-glucoamylase and sucrase-isomaltase complexes from the crude mixture of the rat alpha-glucosidases, the inhibitory activities of the galloylglucose derivatives against each complex were examined. The inhibitory influence on the maltase-glucoamylase complex was more potent than on the sucrase-isomaltase complex.

    Topics: Animals; Biphenyl Compounds; Gallic Acid; Glucose; Glucosides; Glycoside Hydrolase Inhibitors; Hydrolyzable Tannins; Molecular Structure; Rats; Tannins

2001
A study on the nitric oxide production-suppressing activity of sanguisorbae radix components.
    Biological & pharmaceutical bulletin, 2000, Volume: 23, Issue:6

    The active components of an aqueous extract of Sanguisorbae Radix, which possesses nitric oxide (NO) production-suppressing activity, were determined using macrophages that were activated by the addition of lipopolysaccharide. Significant inhibitory activity against the formation of both NO and inducible NO synthase, and NADPH-diaphorase activity, which is involved in NO generation, was shown by Sanguisorbae Radix fractions T-B and T-C. On further fractionation, the subfractions of T-B and T-C all showed high anti-NO activity. Sanguiin H-6, sanguiin H-11, 1,2,3,4,6-penta-O-galloyl-beta-D-glucose, eugeniin and polymeric proanthocyanidin were isolated from TB-3 and TC-4, and all were identified as exhibiting strong anti-NO activity. We have confirmed that sanguiin H-6 is the most active component of Sanguisorbae Radix with respect to the suppression of NO production. It is suggested that tannin makes a prominent contribution to the biological activity of Sanguisorbae Radix.

    Topics: Animals; Anthocyanins; Cells, Cultured; Drugs, Chinese Herbal; Gallic Acid; Glucosides; Hydrolyzable Tannins; Magnetic Resonance Spectroscopy; Male; Mice; Mice, Inbred BALB C; NADPH Dehydrogenase; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Proanthocyanidins; Spectrometry, Mass, Fast Atom Bombardment; Tannins

2000
chemdatabank.com