5-aminolevulinate dehydratase activity in thylakoid-related structures of etiochloroplasts from radish cotyledons

5-Aminolevulinate dehydratase activity was studied in etiochloroplasts purified from radish cotyledons grown for 120 hr under continuous far-red light. The activity was mainly recovered from the stroma of the organelles, as previously observed, but also from the membrane fraction. The bound activity...

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Published inPhytochemistry (Oxford) Vol. 27; no. 5; pp. 1289 - 1295
Main Authors Nasri, F., Huault, C., Balangé, A.P.
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier Ltd 1988
Elsevier
Subjects
5-aminolevulinate dehydratase
Analytical, structural and metabolic biochemistry
Biological and medical sciences
chlorophylls
cotyledons
Cruciferae
enzyme activity
Enzymes and enzyme inhibitors
etiochloroplasts
etioplasts
Fundamental and applied biological sciences. Psychology
Lyases
morphogenesis
Oxidoreductases
phytochrome
porphobilinogen synthase
Raphanus sativus
Rhaphanus sativus
thylakoids
phytochrome
morphogenesis
5-aminolevulinate dehydratase
Cruciferae
chlorophylls
thylakoids
etiochloroplasts
Rhaphanus sativus
Porphobilinogen synthase
Vegetals
Cotyledon
Enzyme
Dicotyledones
Angiospermae
Spermatophyta
Thylakoid
Raphanus sativus
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Summary:5-Aminolevulinate dehydratase activity was studied in etiochloroplasts purified from radish cotyledons grown for 120 hr under continuous far-red light. The activity was mainly recovered from the stroma of the organelles, as previously observed, but also from the membrane fraction. The bound activity was not altered after incubation in the presence of NaCl or detergents indicating that the enzyme was neither associated with the pelletable fraction by electrostatic forces nor entrapped in lipid vesicles. After separation of prothylakoids and prolamellar bodies on a sucrose gradient, 5-aminolevulinate dehydratase activity and two-thirds of the total protein were observed in prothylakoids. Carotenoids were mainly present in the prolamellar bodies fraction. A few chlorophylls were observed in prothylakoids and prolamellar bodies, indicating that impure fractions were obtained, but that 5-aminolevulinate dehydratase activity was actually bound to thylakoid-related structures.
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ISSN:0031-9422
1873-3700
DOI:10.1016/0031-9422(88)80179-1