Phenylalanine ammonia-lyase and chalcone synthase in glands ofPrimula kewensis (W. Wats): immunofluorescence and immunogold localization |
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Authors: | H Schöpker M Kneisel L Beerhues H Robenek R Wiermann |
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Institution: | (1) Institut für Botanik, Universität Münster, Schlossgarten 3, D-48149 Münster, Germany;(2) Institut für Pharmazeutische Biologie, Universität Bonn, Nussallee 6, D-53115 Bonn, Germany;(3) Institut für Arterioskleroseforschung, Abteilung für Zellbiologie und Ultrastrukturforschung, Universität Münster, Domagkstrasse 3, D-48149 Münster, Germany |
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Abstract: | Phenylalanine ammonia-lyase (PAL) and chalcone synthase (CHS) were localized by indirect immunofluorescence and immunogold labeling in glands ofPrimula kewensis. Both enzymes were exclusively present in the head cells of the glands. Phenylalanine ammonialyase was located in the regions of the dense tubular endoplasmic reticulum and occasionally found in more or less spherical organelles that have not yet been identified. Furthermore, an appreciable proportion of the enzyme protein was associated with the plasmalemma and the cell wall of the head cell. In contrast, the occurrence of CHS was restricted to the spherical, unidentified cell compartments. Our findings indicate that the gland cells have the potential for flavonoid biosynthesis. When a mutant ofP. kewensis forming structurally intact glands but incapable of farina excretion was studied, neither PAL nor CHS were found in the head cells.Abbreviations CHS
chalcone synthase
- IgG
immunoglobulin G
- PAL
phenylalanine ammonia-lyase
Financial support from the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie is gratefully acknowledged. We are grateful to Mrs. Karin Schlattmann and Mrs. Susanne Otter for preparing the ultrathin sections and to Mrs. Marianne Opalka for taking the photographs. |
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Keywords: | Chalcone synthase Farina Flavonoid biosynthesis Gland Phenylalanine ammonia-lyase |
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