Purification, properties and kinetic mechanism of flavonol 8-O-methyltransferase from Lotus corniculatus L.
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چکیده
منابع مشابه
Partial purification, kinetic analysis, and amino acid sequence information of a flavonol 3-O-methyltransferase from Serratula tinctoria.
Serratula tinctoria (Asteraceae) accumulates mainly 3,3'-dimethylquercetin and small amounts of 3-methylquercetin as an intermediate. The fact that 3-methylquercetin rarely accumulates in plants in significant amounts, and given its important role as an antiviral and antiinflammatory agent that accumulates in response to stress conditions, prompted us to purify and characterize the enzyme invol...
متن کاملThe Flavonoids of Lotus corniculatus
Since the first studies published in the fifties and sixties (Nakaoki et al., 1956; Harney and Grant, 1964; Bate-Smith, 1965), many authors have investigated the flavonoid chemistry of Lotus corniculatus (Table 1 and Table 2) and demonstrated the richness and diversity of flavonoid compounds in this species. Some authors have examined the variation with altitude of the flavonoid content of Lotu...
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A novel glucosyltransferase which catalyzed the transfer of glucose from UDP-glucose to positions 2' and 5' of partially methylated flavonols was isolated from the shoots of Chrysosplenium americanum Schwein ex Hooker. It was purified 225-fold by ammonium sulfate precipitation and successive chromatography on Sephadex G-100, hydroxyapatite, and polybuffer ion exchanger. This glucosyltransferase...
متن کاملPurification and kinetic mechanism of S-adenosylmethionine: myelin basic protein methyltransferase from bovine brain.
The enzyme S-adenosylmethionine (AdoMet): myelin basic protein (MBP) methyltransferase was purified 250-fold from bovine brain with an overall yield of 130%, relative to crude supernatant. The purification involves acid-base and (NH4)2SO4 precipitation, chromatography over Sephadex G-100 and DEAE-cellulose, followed by preparative isoelectric focusing. The enzyme has a pI of 5.60 +/- 0.05, and ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1985
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1985.tb09304.x