caa a22 4500 477101178 CHVBK 20180405111542.0 cr unu---uuuuu 170330e19960201xx s 000 0 eng 10.1007/BF00206255 doi (NATIONALLICENCE)springer-10.1007/BF00206255 Lipid-body lipoxygenase is expressed in cotyledons during germination prior to other lipoxygenase forms [Elektronische Daten] [Ivo Feussner, Bettina Hause, Arndt Nellen, Claus Wasternack, Helmut Kindl] Lipid bodies are degraded during germination. Whereas some proteins, e.g. oleosins, are synthesized during the formation of lipid bodies of maturating seeds, a new set of proteins, including a specific form of lipoxygenase (LOX; EC 1.13.11.12), is detectable in lipid bodies during the stage of fat degradation in seed germination. In cotyledons of cucumber (Cucumis sativus L.) seedlings at day 4 of germination, the most conspicuous staining with anti-LOX antibodies was observed in the cytosol. At very early stages of germination, however, the LOX form present in large amounts and synthesized preferentially was the lipid-body LOX. This was demonstrated by immunocytochemical staining of cotyledons from 1-h and 24-h-old seedlings: the immunodecoration of sections of 24-h-old seedlings with anti-LOX antiserum showed label exclusively correlated with lipid bodies of around 3 μm in diameter. In accordance, the profile of LOX protein isolated from lipid bodies during various stages of germination showed a maximum at day 1. By measuring biosynthesis of the protein in vivo we demonstrated that the highest rates of synthesis of lipid-body LOX occurred at day 1 of germination. The early and selective appearance of a LOX form associated with lipid bodies at this stage of development is discussed. Springer-Verlag, 1996 Cucumis nationallicence Germination nationallicence Lipid body (immunocytochemical staining) nationallicence Lipoxygenase nationallicence Protein synthesis (in vivo) nationallicence DAPI : 4,6-diamidino-2-phenylindole nationallicence DIC : differential interference contrast nationallicence FITC : fluorescein-5-isothiocyanate nationallicence LOX : lipoxygenase nationallicence Feussner Ivo Fachbereich Chemie, Philipps-Universität, D-35032, Marburg, Germany aut Hause Bettina Institut für Pflanzenbiochemie, Weinberg 3, D-06120, Halle, Germany aut Nellen Arndt Fachbereich Chemie, Philipps-Universität, D-35032, Marburg, Germany aut Wasternack Claus Institut für Pflanzenbiochemie, Weinberg 3, D-06120, Halle, Germany aut Kindl Helmut Fachbereich Chemie, Philipps-Universität, D-35032, Marburg, Germany aut Planta Springer-Verlag 198/2(1996-02-01), 288-293 0032-0935 198:2<288 1996 198 425 https://doi.org/10.1007/BF00206255 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00206255 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Feussner Ivo Fachbereich Chemie, Philipps-Universität, D-35032, Marburg, Germany aut NATIONALLICENCE 700 1- Hause Bettina Institut für Pflanzenbiochemie, Weinberg 3, D-06120, Halle, Germany aut NATIONALLICENCE 700 1- Nellen Arndt Fachbereich Chemie, Philipps-Universität, D-35032, Marburg, Germany aut NATIONALLICENCE 700 1- Wasternack Claus Institut für Pflanzenbiochemie, Weinberg 3, D-06120, Halle, Germany aut NATIONALLICENCE 700 1- Kindl Helmut Fachbereich Chemie, Philipps-Universität, D-35032, Marburg, Germany aut NATIONALLICENCE 773 0- Planta Springer-Verlag 198/2(1996-02-01), 288-293 0032-0935 198:2<288 1996 198 425 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer