The estimation of phenylalanine ammonia-lyase (PAL)-activity in intact cells of higher plant tissue |
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Authors: | Nikolaus Amrhein Karl-Heinz Gödeke |
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Affiliation: | (1) Lehrstuhl für Biochemie der Pflanzen, Biologisches Institut II, Universität Freiburg, Schänzlestr. 9/11, D-7800 Freiburg, Federal Republic of Germany;(2) Present address: National Research Center Cairo, Egypt |
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Abstract: | From cell cultures of Haplopappus gracilis, an enzyme, catalyzing the glucosylation of cyanidin at the 3 position using uridine diphosphate-D-glucose (UDPG) as glucosyl-donor, has been isolated and purified 50-fold. The enzyme was not specific for cyanidin alone, but also glucosylated other anthocyanidins and flavonols in position 3. However, apigenin, luteolin, naringenin and dihydroquercetin were not glucosylated. The reaction has an optimum pH of approximately 8, and the apparent Km values for UDPG and cyanidin were 0.5 and 0.33 mM respectively. The enzyme reaction is strongly inhibited by cyanidin (above 0.25 mM). |
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Keywords: | UDP-glucose Glucosyltransferase Cyanidin Anthocyanidin Flavonol Haplopappus |
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