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chrysosplenium grayanum/flavonoid

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To control the quality of Chrysosplenium alternifolium L., a simple, fast and reliable method of high-performance liquid chromatography coupled with a photodiode array detector (HPLC-PDA) was developed and validated for simultaneous quantitative determination of four bioactive polymethoxylated

Tissue culture of Chrysosplenium americanum and its potential for flavonoid production.

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Chrysosplenium americanum (Saxifragaceae) accumulates a variety of partially O-methylated flavonol glucosides. Because of the semi-aquatic nature of this plant and its extensive contamination with endogenous organisms, the initiation of shoot and callus cultures could only be achieved after (a)

Isolation and cytotoxicity of two new flavonoids from Chrysosplenium grayanum and related flavonols.

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In view of the observation that a CHCl3-soluble fraction of the MeOH extract of Chrysosplenium grayanum has shown cytotoxic activity in the KB cell in vitro system, the fraction has been further fractionated to furnish five known flavonoids (chrysosplenols B, D, and E, retusin, and brickellin),
BACKGROUND Gastric cancer remains highly prevalent, but treatment options are limited. Natural products have proved to be a rich source of anticancer drugs. Chrysosplenium nudicaule Ledeb. (Saxifragaceae) is a perennial herb that grows in the highlands of China. It has been used as a traditional
Enzymatic O-methylation of phenylpropanoid and flavonoid compounds is believed to be catalyzed by distinct classes of O-methyltransferases [EC 2.1.1.6x]. The O-methylated derivatives of phenylpropanoids and flavonoids play an important role in lignification and as antimicrobial compounds,
The steady-state kinetic behavior of three position-specific O-methyltransferases (3-, 4'-, and 6-OMTs) was compared with reference to substrate inhibition patterns in Chrysosplenium americanum. The 6-OMT was severely inhibited by the flavonoid substrate at concentrations close to Km, whereas the

Role of Serine 286 in cosubstrate binding and catalysis of a flavonol O-methyltransferase.

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O-Methyltransferases catalyze the transfer of the methyl groups of S-adenosyl-L-methionine to specific hydroxyl groups of several classes of flavonoid compounds. Of the several cDNA clones isolated from a Chrysosplenium americanum library, FOMT3' encodes the 3'/5'-O-methylation of partially

Molecular characterization and functional expression of flavonol 6-hydroxylase.

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BACKGROUND Flavonoids, one of the major groups of secondary metabolites, play important roles in the physiology, ecology and defence of plants. Their wide range of activities is the result of their structural diversity that encompasses a variety of functional group substitutions including
A 2-oxoglutarate-dependent dioxygenase [EC 1.14.11-] that catalyzes the 6-hydroxylation of partially methylated flavonols has been purified to near homogeneity from Chrysosplenium americanum. Enzyme purification was achieved by fast protein liquid chromatography on Superose 12 and Mono Q columns as
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