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  • 1
    Electronic Resource
    Electronic Resource
    Changes in blue-light-dependent protein phosphorylation during the early development of etiolated oat seedlings (1996)
    Springer
    Planta 199 (1996), S. 336-342 
    Details
    ISSN: 1432-2048
    Keywords: Avena ; Photoreceptor ; Phototropism ; Plasma membrane ; Protein kinase ; Protein phosphorylation (blue-light-dependent)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Blue light induced the phosphorylation of a 116-kDa plasma-membrane-associated protein in dark-grown seedlings from Avena sativa L. The response was restricted to the phototropically sensitive tissue of the coleoptile tip. Surprisingly, this protein showed different properties in membrane preparations from plants that were grown for 3 d than in those from 5-d-old seedlings. In contrast to the younger coleoptiles, in 5-d-old seedlings phosphorylation of the 116-kDa protein depended strictly on the addition of Triton X-100 or other non-ionic detergents and was not abolished when the membranes were pretreated with trypsin. These latter membranes were also characterized by the appearance of two additional bluelight-regulated phosphoproteins of slightly lower molecular masses, exhibiting properties similar to the 116-kDa protein from 3-d-old plants. The data, together with solubilization studies, indicate that the 116-kDa protein is strongly membrane-bound only at the very beginning of seedling development and becomes more loosely associated in the course of coleoptile growth. In addition, we demonstrate that the capacity of the light-activated photoreceptor to recover photosensitivity in the dark also can occur under in-vitro conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00195724
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  • 2
    Electronic Resource
    Electronic Resource
    Chlorophyll b reduction during senescence of barley seedlings (1999)
    Springer
    Planta 209 (1999), S. 364-370 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Chlorophyllase ; Chlorophyll b reductase ; Hordeum ; 71-Hydroxy-chlorophyll a ; Leaf senescence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. During senescence of flowering plants, only breakdown products derived from chlorophyll a were detected although  b disappears, too (Matile et al., 1996, Plant Physiol 112: 1403–1409). We investigated the possibility of chlorophyll b reduction during dark-induced senescence of barley (Hordeum vulgare L.) leaves. Plastids isolated from senescing leaves were lysed and incubated with NADPH. We found 71-hydroxy-chlorophyll a, 71-hydroxy-chlorophyllide a, and, after incubation with Zn-pheophorbide b, also Zn-71-hydroxy-pheophorbide a, indicating activity of chlorophyll(ide) b reductase. The highest activity was found at day 2 of senescence when chlorophyll breakdown reached its highest rate. Chlorophyllase reached its highest activity under the same conditions only at days 4–6 of senescence. Based on the chlorophyll b reductase activity of plastids at day 2.5 of senescence (=100%), the bulk of activity (83%) was found in the thylakoids and only traces (5%) in the envelope fraction. Chlorophyll b reduction is considered to be an early and obligatory step of chlorophyll b breakdown.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050644
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  • 3
    Electronic Resource
    Electronic Resource
    Incorporation of phytol precursors into chlorophylls of tobacco cell cultures (1984)
    Springer
    Planta 162 (1984), S. 215-219 
    Details
    ISSN: 1432-2048
    Keywords: Chlorophyll biosynthesis ; Nicotiana (chlorophyll biosynthesis) ; Geranylgeranyl phosphate ; Phytol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The incorporation of [1-3H] geranylgeranyl diphosphate (GGPP), [1-3H] geranylgeranyl monophosphate (GGMP) and [U-14C] phytyl diphosphate (PhPP) into chlorophylls a and b in growing tobacco cell cultures was investigated. The substrates were effectively incorporated into chlorophylls a and b, 3.2% of the total activity of applied GGPP or GGMP and 12.4% of the total activity of applied PhPP being found in chlorophylls a and b after 24 h incubation. The radioactivity was found in phytyl chlorophyllide through-out which means effective hydrogenation of the alcohol moiety in the case of GGPP and GGMP. With increasing substrate concentration, the specific radioactivity of chlorophyll increased up to a saturation level which was reached either at 20–40 μM PhPP or at 60 μM GGPP and GGMP. The specific radioactivity of the chlorophyll formed during the 24-h incubation period was the same as that of the applied substrate at saturating substrate concentration. The specific radioactivity of chlorophyll a was higher than that of chlorophyll b only in the case of PhPP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00397442
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  • 4
    Electronic Resource
    Electronic Resource
    Chlorophyll biosynthesis by mesophyll protoplasts and plastids from etiolated oat (Avena sativa L.) leaves (1981)
    Springer
    Planta 152 (1981), S. 54-58 
    Details
    ISSN: 1432-2048
    Keywords: Avena ; Chlorophyll biosynthesis ; Etioplasts ; Geranylgeranyldiphosphate ; Protoplasts
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The uptake of [1-3H]geranylgeranyl diphosphate (GGPP) into protoplasts and intact etioplasts and the metabolic interconversion therein was studied after a 2 min pulse of white light. The chlorophyll synthetase reaction, Chlide+GGPP→ChlGG, was taken as a natural probe for the etioplast compartment. This reaction yields labeled ChLGG and, by hydrogenation, labeled ChlP, when [1-3H]GGPP receives access to the etioplast stroma. It was found that penetration across the plastid envelope was rapid and that penetration across the plasma membrane of protoplasts, however, was slow. A cellular pool of soluble GGPP was detected. This pool was lost, in part, during preparation of the protoplasts and almost completely during preparation of the etioplasts. The membrane-bound phytol pool of etioplasts could not be replaced by exogenous [3H]GG. The endogenous GG and phytol pools of protoplasts, which were larger than those of etioplasts, could be replaced in part by exogenous [3H]GGPP. That part of this pool exists as soluble GGPP or as a direct precursor in the cytoplasm is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00384985
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  • 5
    Electronic Resource
    Electronic Resource
    Investigations on the apoprotein of phycocyanin from Cyanidium caldarium (1983)
    Springer
    Archives of microbiology 135 (1983), S. 30-35 
    Details
    ISSN: 1432-072X
    Keywords: Rhodophyta ; Cyanidium caldarium ; Biliprotein ; Levulinic acid ; δ-aminolevulinic acid incorporation ; Phycocyanin apoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cultures of the unicellular red alga Cyanidium caldarium were transferred from heterotrophic growth conditions to photoautotrophic growth. During photoautotrophic growth, the biliprotein phycocyanin is synthesized de novo. In the presence of 2–5 mM/l levulinic acid which inhibits the biosynthesis of tetrapyrrole chromophores, phycocyanin biosynthesis is suppressed by a factor of 29. Immunoprecipitation yields small amounts of “apoprotein” i.e. phycocyanin which lacks all or part of its chromophore(s). In various experiments the ratio apoprotein/residual holoprotein (phycocyanin) was determined as 2–6 to one. Incubation with [3H]leucine leads to labelled immunoprecitable material: apoprotein (18,300–19,600 Mr) and larger poly-peptides (50,000–52,000 Mr) of unknown nature. The apoprotein was separated from residual phycocyanin by chromatography on DEAE-cellulose and preparative isoelectric focusing (IEF). The significance of the results for further studies on the last steps of phycocyanin biosynthesis is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00419478
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  • 6
    Electronic Resource
    Electronic Resource
    Investigation of C-phycoerythrin from the cyanobacterium Pseudanabaena W 1174 (1980)
    Springer
    Archives of microbiology 127 (1980), S. 253-257 
    Details
    ISSN: 1432-072X
    Keywords: Pseudanabaena strains ; C-phycoerythrin ; Chromatic adaptation ; Proteolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cyanobacterium which produces high amounts of C-phycoerythrin was classified as a new Pseudanabaena strain. This strain (number W 1173 of our collection) has been cultivated for 6 years without changing its properties. It resembles Pseudanabaena catenata (strain B 1464-1) morphologically but differs in the pigmentation. Contrary to strain B 1464-1, no chromatic adaptation was observed with strain W 1173. It was found that phycoerythrins from both strains differ in the following properties: isoelectric points, number of bilin chromophores, and immunochemical properties. Besides native C-phycoerythrin (PEI, λmax = 558 nm), a degradation product (PEII, λmax = 544 nm and 562nm) has been found in crude extracts from strain W 1173. Criteria for integrity of C-phycoerythrin were discussed which are essential if this biliprotein is used as taxonomic character.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00427201
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