| 1 | Author
| Rainer Sütfeld, Rolf Wiermann | Requires cookie* | | Title
| Purification of Chalcone Synthase from Tulip Anthers and Comparison with the Synthase from Cosmos Petals  | | | Abstract
| Chalcone synthase was isolated from both anthers of Tulipa cv. "A peldoorn" and petals of Cosmos sulphureus Cav. After certain prepurification steps, the enzymes were further purified using gel chrom atography on Sephadex G-200 followed by repeated hydroxylapatite absorption chromatography. Both the enzymes showed the same chrom atographic properties. After gel chrom atography as well as after the first hydroxylapatite fractionation, the reaction products appeared as flavanones. However, after the second hydroxylapatite step, production of chalcones was observed. Like the enzyme from tulip anthers, the synthase from Cosmos petals produced the correspondingly substituted chalcones when p-coumaroyl-CoA, caffeoyl-CoA and feruloyl-CoA, respectively, were used as substractes. In both the cases, the ratios o f the different chalcones produced were found to be about the same. The appearance o f chalcone synthesis in this in vitro assay is caused by the complete elim ination of chalcone isomerase in the purification procedure. The importance of the isomerase for flavonoid biosynthesis, particularly in plant systems which are accumulating chalcones, is discussed. | | |
Reference
| Z. Naturforsch. 36c, 30—3 (1981); received N ovem ber 12 1980 | | |
Published
| 1981 | | |
Keywords
| Tulipa, Cosmos, Biosynthesis, Flavonoids, Chalcone Synthase | | |
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| default:Reihe_C/36/ZNC-1981-36c-0030.pdf | | | Identifier
| ZNC-1981-36c-0030 | | | Volume
| 36 | |
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