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δ-Aminolevulinate dehydratase from Raphanus sativus cotyledons
Authors:AP Balange  C Lambert
Institution:Laboratoire de Photobiologie (Laboratoire associé au C.N.R.S. L.A 203), Centre de Recherche de Biochimie et Physiologie Cellulaires, Faculté des Sciences, B.P. 67, 76130 Mont Saint Aignan, France
Abstract:Phytochrome induces δ-aminolevulinate dehydratase (ALAD) activity in radish seedling cotyledons under continuous far red light. Analysis of the enzymatic activity in etioplasts vs total activity shows a constant ALAD level in these organelles (10 %) in etiolated seedlings. In far red irradiated seedlings, the percentage of enzyme detected into etioplasts increases up to 45 % of the total. Comparative kinetic studies of ALAD activity detected in the cytoplasm and the etioplasts indicate an increase in both compartments with a maximum value reached respectively at 96 and 120 hr from sowing. Treatment with cycloheximide shows a very fast abolition of cytoplasmic ALAD activity which is always correlated to an etioplast decrease with a time shift of ca 24 hr. Erythromycin acts only on the cytoplasmic level of ALAD, and only for far red irradiated seedlings, with an increase of activity twice the level detected in untreated ones. This unexpected effect is discussed.
Keywords:Cruciferae  δ-aminolevulinate dehydratase  phytochrome  cycloheximide  etioplasts  erythromycin    δ-ALA—δ-aminolevulinic acid: ALAD—δ-aminolevulinic acid dehydratase (EC  4  2  1  24)  FR—standard far red light (λ ? 720 nm)  PBG—porphobilinogen  CHI—cycloheximidine  ERT—erythromycin  
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