Accumulation of a 50-kDa protein during leaf senescence of alstroemeria cut flowering stems
| Autor: | G. M. Stoopen, W. Jordi, E. in ‘t Veld, P. Heinen, I. Argiroudi, H. van Tol |
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| Jazyk: | angličtina |
| Rok vydání: | 1996 |
| Předmět: |
Senescence
Chlorophyll 3-Isopropylmalate Dehydrogenase Physiology Instituut voor Agrotechnologisch Onderzoek Plant Science Biology chemistry.chemical_compound Alstroemeria Botany Genetics medicine Gibberellic acid 2D-electrophoresis Research Institute for Agrobiology and Soil Fertility fungi food and beverages Instituut voor Agrobiologisch en Bodemvruchtbaarheidsonderzoek Cell Biology General Medicine Polypeptide pattern Trypsin biology.organism_classification Isoelectric point chemistry Biochemistry Agrotechnological Research Institute Leucine medicine.drug |
| Zdroj: | Physiologia Plantarum 98 (1996) Physiologia Plantarum, 98, 819-823 |
| ISSN: | 0031-9317 |
| Popis: | Leaf senescence of alstroemeria cut flowering stems in the dark was accompanied by a decrease in the soluble protein and chlorophyll content. Two-dimensional (2D) electrophoresis revealed that a polypeptide with an apparent molecular mass of 50 (± 2) kDa and isoelectric point of 5.0 (± 0.1) accumulated during the senescence process. Treatments which delayed leaf senescence (light and gibberellic acid) diminished the accumulation of this polypeptide. This polypeptide was purified and one of the peptides, resulting from digestion with trypsin, was sequenced. The se quence shows a high degree of homology to that of 3-isopropylmalate dehydrogenase. This enzyme plays a role in the biosynthesis of leucine. Possibly, leucine plays a role in carbon partitioning between sources and sinks in this plant. |
| Databáze: | OpenAIRE |
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