| | 1 | Author
| SachioW. Akayam, K. Azuhito, K. Usaka, T. Sutom, K. Anehira, Y. Asuyuki, Y. Am Ada, Kazuyoshi Kawazu, A. Kio, K. Obayashi | Requires cookie* | | | Title
| Kinobeon A, A Novel Red Pigment Produced in Safflower Tissue Culture Systems  | | | | Abstract
| The production of safflower pigments by tissue culture techniques was carried out using the calh induced from various parts of the plant. After massive cell selection efforts, a cul ture cell line (KB 7) was found to produce a considerable amount of a red pigment. Addi tion of cellulose powder and D-phenylalanine into the medium dramatically improved the pigment production. After purification, red crystals were obtained. Its UV/VIS spectrum as well as the HPLC behavior was clearly different from that of carthamin found in the mother plant and those of another typical plant pigments, suggesting that it was a novel compound. Therefore, this pigment was named kinobeon A. | | | |
Reference
| Z. Naturforsch. 49c, 1—5 (1994); received October 12/November 111993 | | | |
Published
| 1994 | | | |
Keywords
| Kinobeon A, Red Pigment, Safflower, Carthamus tinctorius, Plant Tissue Culture | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0001.pdf | | | | Identifier
| ZNC-1994-49c-0001 | | | | Volume
| 49 | |
| 3 | Author
| H. Lert, K. T. Araz, H. Budzikiewicz | Requires cookie* | | | Title
| Serratiochelin, a New Catecholate Siderophore from Serratia marcescens | | | | Abstract
| The catecholate siderophore serratiochelin isolated from an iron deficient culture medium of Serratia marcescens TW was characterized by mass spectrometry and NMR and by GC/MS analysis of the hydrolysis products as l-(2,3-dihydroxybenzamido)-3-[4 S,5i?-2-(2,3-dihy-droxyphenyl)-5-methyl-2-oxazoline-4-carboxamido]propane. The structure of serratiochelin was confirmed by synthesis. The bacterial strain also produces chrysobactin. In tro d u ctio n | | | |
Reference
| Z. Naturforsch. 49c, 11—17 (1994); received October ll/D ecem ber 201993 | | | |
Published
| 1994 | | | |
Keywords
| Catecholate Siderophore, Serratiochelin, Chrysobactin, Structure Elucidation, Serratia marcescens | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0011.pdf | | | | Identifier
| ZNC-1994-49c-0011 | | | | Volume
| 49 | |
| 5 | Author
| R. Ainer, D. Eutzm Ann | Requires cookie* | | | Title
| Purification and Properties of Acridone Synthase from Cell Suspension Cultures of Ruta gvaveolens L | | | | Abstract
| Rutaceae, Ruta graveolens, Acridone Synthase, Microsequencing, Alkaloids Acridone synthase has been purified from cell suspension cultures of Ruta graveolens using a combination of gel filtration and ion exchange chromatography. The purified enzyme has an apparent molecular weight of 69 kDa on gel filtration and a subunit structure on SDS-PAGE of 40 kDa. The apparent A^m-values are 10.64 |iM and 32.8 |iM for N-methylanthraniloyl-CoA and malonyl-CoA, respectively. Tryptic digestion of the homogeneous acridone synthase was performed. Seven of the peptides were chosen for microsequencing. The homology of the amino acid sequences from this particular polypeptide and corresponding peptides from chal-cone synthase 3 from garden pea amounted to 76%. | | | |
Reference
| Z. Naturforsch. 49c, 26—32 (1994); received September lO/October 14 1993 | | | |
Published
| 1994 | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0026.pdf | | | | Identifier
| ZNC-1994-49c-0026 | | | | Volume
| 49 | |
| 6 | Author
| Z. Naturforsch | Requires cookie* | | | Title
| Evidence for Nickel in the Soluble Hydrogenase from the Unicellular Green Alga Scenedesmus obliquus | | | | Abstract
| ,1993 Scenedesmus obliquus, Hydrogenase, Nickel Cultures of the green alga Scenedesmus obliquus were grown in the presence of either the chelating reagent ED TA or NiCl2 in various concentrations and assayed for hydrogenase catalyzed photohydrogen evolution after an anaerobic dark adaptation period. Cultivation of algae in the presence of 100 [am EDTA inhibited the formation of hydrogenase activity by 37%. After a cultivation of the cells in the presence of 5 -2 0 [xm NiCl2 photohydrogen evo lution was increased by 20-40% . Addition of EDTA up to a final concentration of 1.5 mM had no effect on the activity of hydrogenase in cell-free hydrogenase preparations. Cultures grown in the presence of radioactive 63NiCl2 incorporated 63Ni in a parallel fashion to the cell growth. In radioactive labeled hydrogenase preparations a co-elution of radioactivity and hydrogenase activity could be observed using gel filtration chro matography. In tro d u ctio n H ydrogenases catalyze th e reversible oxidation of m olecular hydrogen as indicated by the following equation: | | | |
Reference
| Z. Naturforsch. 49c, 33—38 (1994); received November 22 | | | |
Published
| 1994 | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0033.pdf | | | | Identifier
| ZNC-1994-49c-0033 | | | | Volume
| 49 | |
| 7 | Author
| E. Lke Strehl, R. Egina, V. Olpert, E. Rich, F. E. Lstn Er | Requires cookie* | | | Title
| Biochemical Activities of Propolis-Extracts m . Inhibition of Dihydrofolate Reductase | | | | Abstract
| Propolis, Dihydrofolate Reductase, Antiinflammatory Drugs, Caffeic Acid Ethanolic and aqueous extracts of the natural compound PROPOLIS indicate substanti al antiinflammatory functions as well as antibiotic activities in vitro and in vivo. The exact mode of physiological or biochemical mechanisms responsible for the medical effects, ho wever, is all but clear. The standardization on the basis of quantitative determination of pro minent components of these extracts have been substituted recently by simple biochemical model reactions including photodynamic properties. In this communication we report on the inhibitory activity of an aqueous extract of propolis on the enzyme dihydrofolate reductase. This activity may at least partially be due to the content of caffeic acid, as revealed by HPLC chromatography and comparative activity tests of representative ingredients of the propolis extract. This result may explain some of the protective functions of propolis, similar to those shown for several "non-steroidal antiinflammatory drugs", NSAIDs. | | | |
Reference
| Z. Naturforsch. 49c, 39—43 (1994); received August 16/October 151993 | | | |
Published
| 1994 | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0039.pdf | | | | Identifier
| ZNC-1994-49c-0039 | | | | Volume
| 49 | |
| 9 | Author
| Y. Ukih, Aru Sato, T. O. Shinobu, H. Oshi, T. Etsuji Iida, Chifuyu Ogino, B. Eate Nicolaus, W. Akabayashi, P. E. Te, R. Böger | Requires cookie* | | | Title
| Isomerization and Peroxidizing Phytotoxicity of Thiadiazolidine Herbicides | | | | Abstract
| Certain 5-(arylimino)-3,4-tetramethylene-l,3,4-thiadiazolidin-2-ones (thiadiazolidines) are peroxidizing bleaching herbicides which interrupt chlorophyll biosynthesis, inhibit the activity of protoporphyrinogen oxidase, lead to accumulation of protoporphyrin IX, and induce ethane formation in the light. The same effects are caused by their isomers, the 4-aryl-l,2-tetramethylene-l,2,4-triazolidin-3-one-5-thiones (triazolidines). Couples of thia diazolidines and corresponding triazolidine isomers were synthesized. Thiadiazolidines with a 4-bromophenylimino, 4-chlorophenylimino, 4-chloro-2-methylphenylimino, 4-chloro-2-fluorophenylimino, 4-chloro-2-fluoro-5-propargyloxyphenylimino and 4-chloro-2-fluoro-5-isopropoxyphenylimino moiety were converted to the corresponding triazolidines both with Echinochloa seedlings or a spinach homogenate present, depending on the 5-arylimino moiety. The 5-[4-(chlorobenzyloxy)phenylimino]-3,4-tetramethylene-l,3,4-thiadiazolidin-2-one analogue did not convert to the corresponding triazolidine under both conditions. Thiadiazolidines as well as triazolidines having a 4-chloro-2-fluoro-5-methoxycarbonyl-methylthiophenyl moiety were converted to an unidentified compound whose structure is assumed to be 4-(4-chloro-2-fluoro-5-carboxymethylthiophenyl)-l,2-tetramethylene-l,2,4-triazolidin-3-one-5-thione. Apparently, the general conversion mechanism is caused by enzymatic hydrolysis of thiadiazolidines to an unstable intermediate which rapidly and spon taneously changes to the corresponding triazolidine isomer. | | | |
Reference
| Z. Naturforsch. 49c, 49 (1994); received November 121993 | | | |
Published
| 1994 | | | |
Keywords
| Proherbicide, Isomerization, Triazolidinonethiones, Thiadiazolidinones, Echinochloa | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0049.pdf | | | | Identifier
| ZNC-1994-49c-0049 | | | | Volume
| 49 | |
| 10 | Author
| Thomas Steger-Hartmann, Ulrich Koch, Thomas Dunz, EdgarW. Agner | Requires cookie* | | | Title
| Induced Accumulation and Potential Antioxidative Function of Rutin in Two Cultivars of Nicotiana tabacum L | | | | Abstract
| ,1993 Tobacco, Flavonoids, Ozone, Antioxidants, UV The rutin (quercetin-3-rhamnosyl-glucoside) content of two tobacco cultivars (Nicotiana tabacum L.) which differ in their ozone-sensitivity was assayed after exposure to various rutin-inducing stimuli. In the growth-chamber, UV radiation in combination with white light led to the accumulation of similar amounts of rutin in both cultivars. Treatment with radical pro ducing agents (terf-butylhydroperoxide and paraquat) also led to rutin accumulation. In this case, the rutin content was higher in the tolerant cultivar. The rutin content was also higher in the tolerant cultivar upon exposure of the plants on an out-door stand, even when the UV-part of the sun spectrum was excluded by cut-off filters. The potential role of rutin as antioxidant was tested with an ion leakage assay. Plants with relatively high rutin content were less sensitive towards paraquat-induced ion leakage than plants without rutin. Thus, the higher rutin content of the ozone-tolerant cultivar Bel B may well contribute to its tolerance against oxidative stress. | | | |
Reference
| Z. Naturforsch. 49c, 57—62 (1994); received August 27/October 18 | | | |
Published
| 1994 | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0057.pdf | | | | Identifier
| ZNC-1994-49c-0057 | | | | Volume
| 49 | |
| 11 | Author
| M. Stolz, D. D. Örnem Ann | Requires cookie* | | | Title
| Purification, Characterization and N-Terminal Sequence of Phosphoserine Aminotransferase from the Green Alga Scenedesmus obliquus, Mutant C-2 A | | | | Abstract
| Scenedesmus obliquus, Phosphorylated Pathway, Phosphoserine Aminotransferase Phosphoserine aminotransferase (EC 2.6.1.52), an enzyme of the "phosphorylated path way" leading to the formation of serine, was purified from Scenedesmus obliquus, mutant C-2 A '. Purification started from the soluble supernatant of a crude cell homogenate and in cluded different affinity and DEAE chromatographic techniques, as well as gel filtration. The purified phosphoserine aminotransferase was enriched 1537-fold and identified to be a homo dimer with subunit molecular masses of 40 kDa, each. The absorption spectrum is consistent with the presence of pyridoxal-5-phosphate as cofactor. From the purified enzyme 18 amino acids of the N-terminus could be determined, showing at least 67% homology with the serC gene encoding phosphoserine aminotransferases from bacterial organisms. | | | |
Reference
| Z. Naturforsch. 49c, 63—69 (1994); received November 11/December 161993 | | | |
Published
| 1994 | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0063.pdf | | | | Identifier
| ZNC-1994-49c-0063 | | | | Volume
| 49 | |
| 12 | Author
| Ulrike Strohmeier, ChristianG. Erdes3, Wolfgang Lockaub | Requires cookie* | | | Title
| Proteolysis in Heterocyst-Forming Cyanobacteria: Characterization of a Further Enzyme with Trypsin-Like Specificity, and of a Prolyl Endopeptidase from Anabaena variabilis | | | | Abstract
| of the cyanobacterium Anabaena variabilis ATCC 29413 and an en gineered mutant that lacks an intracellular protease cleaving after Lys and Arg (Maldener, Lockau, Cai, and Wolk, Mol. Gen. Genet. 225, 113-120 (1991)) were separated by ion ex change chromatography, and protease profiles determined using azocasein, Na-benzoyl-D,L-arginine-4-nitroanilide and N-carbobenzoxy-glycyl-L-proline-4-nitroanilide as substrates. A second enzyme cleaving at the carboxyl side of lysine and arginine, and a prolyl endopepti dase were detected, enriched and characterized. Both proteolytic enzymes appear to be located in the periplasm. | | | |
Reference
| Z. Naturforsch. 49c, 70—78 (1994); received September 29/December 81993 | | | |
Published
| 1994 | | | |
Keywords
| Anabaena variabilis, Cyanobacterium, Heterocysts, Proteolytic Enzymes, Prolyl Endopeptidase Soluble extracts | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0070.pdf | | | | Identifier
| ZNC-1994-49c-0070 | | | | Volume
| 49 | |
| 13 | Author
| ThiloC. Fischer, Sabine Groner, Ulrike Zentgraf, Vera Hemleben | Requires cookie* | | | Title
| Evidence for Nucleosomal Phasing and a Novel Protein Specifically Binding to Cucumber Satellite DNA | | | | Abstract
| The nucleosomal organization and the protein-binding capability of highly repeated and methylated satellite DNA of cucumber (Cucumis sativus L.), comprising approx. 30% of the genome, were analyzed. Nucleosomal core DNA from satellite type I was prepared after micrococcal nuclease digestion of chromatin and sequenced. Most of the core sequences ob tained could be grouped in two main (A and B) and two minor groups (C and D) indicating a specific and complex phasing of nucleosomes on this satellite DNA. In vitro, gel retarda tion assays with cloned satellite DNA repeats (types I-IV) demonstrated a specific binding of nuclear proteins. These specific binding effects are also obtained with genomic, in vivo methylated and sequence heterogeneous (1 to 10% diversity) satellite type I DNA. For the first time in plants, a satellite DNA-binding protein with an apparent molecular weight of 14 kDa (SAT 14) was identified. | | | |
Reference
| Z. Naturforsch. 49c, 79—86 (1994); received October 28/November 121993 | | | |
Published
| 1994 | | | |
Keywords
| Cucumis sativus, DNA Methylation, DNA-Protein Interaction, Nucleosomal Phasing, Satellite DNA | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0079.pdf | | | | Identifier
| ZNC-1994-49c-0079 | | | | Volume
| 49 | |
| 14 | Author
| KlausP. Bader, SusanneH. Öper | Requires cookie* | | | Title
| Stimulatory Effects of an Ammonium Salt Biocide on Photosynthetic Electron Transport Reactions | | | | Abstract
| Photosynthesis, Electron Transport, Biocide, Quaternary Ammonium Salt Alkylbenzyldimethylammonium chloride (ABDAC, zephirol) has been shown to improve the functioning of the photosynthetic apparatus of the filamentous cyanobacterium Oscillatoria chalybea (Bader, K. P. (1989) Biochim. Biophys. Acta 975, 399-402). This bio cide exerts stimulatory effects on various electron transport reactions in Oscillatoria chaly bea and chloroplasts from higher plants. By means of oxygen evolution measurements and of repetitive flash-induced absorption spectroscopy we were able to demonstrate an impact of the drug on the major complexes of photosynthetic membranes, i.e. the water splitting complex, photosystem II and photosystem I. Both, P820-and X320-absorption change signals were enhanced by the addition of ABDAC. Along with the quantitative analysis we investi gated the relaxation kinetics of the signals and observed a substantial stabilization of the oxi dized states of the respective redox components in the presence of the ammonium salt. Under appropriate conditions the relaxation kinetics of the absorption signals were significantly slowed down. ABDAC also affects photosystem I in Oscillatoria chalybea, but only under conditions, where a donor/acceptor system i.e. an isolated photosystem I reaction with photo system II being disconnected was measured. Electron transport through the whole chain i.e. with water as the electron donor yielded no effect of the quaternary ammonium salt. It is sug gested that this is due to an extremely bad linkage between the two photosystem, each of which, however, shows good reaction rates, when separately measured. The described inter actions of the biocide with photosynthetic membranes are not restricted to Oscillatoria chalybea but are also observed with higher plant chloroplasts. In these systems, ABDAC enhances X320-and P700-signals to a comparable extent. In this case the P700-signal is stimulat ed in assays with electrons which are furnished from water which hints at good coupling be tween the two photosystems in our tobacco chloroplast preparations. | | | |
Reference
| Z. Naturforsch. 49c, 87 (1994); received November 8 1993 | | | |
Published
| 1994 | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0087.pdf | | | | Identifier
| ZNC-1994-49c-0087 | | | | Volume
| 49 | |
| 15 | Author
| M. Athias, R. Uff, ElfriedeK. Pistorius | Requires cookie* | | | Title
| Isolation and Partial Characterization of a Manganese and Chloride Binding Protein Present in Highly Purified Photosystem II Complexes of the Thermo philic Cyanobacterium Synechococcus sp.: The Protein Being Detected by Its L -Arginine Metabolizing Activity | | | | Abstract
| This paper is dedicated to Professor Birgit Vennesland on the occasion o f her 80 th birthday L-Arginine Metabolizing Enzyme, Water Oxidizing Enzyme, Photosystem II, Thermophilic Cyanobacteria, Synechococcus sp. Photosystem II complexes were solubilized with the detergent sulfobetaine 12 from thyla-koid membranes of the thermophilic cyanobacterium Synechococcus sp. and purified by two sucrose gradient centrifugations and by chrom atography on a M ono Q column. In such pho tosystem II complexes having a photosynthetic O, evolving activity o f 2938 |amol 0 2 evolved/ mg chlorophyll x h, an L-arginine metabolizing activity leading to ornithine and urea as major products, could be shown to be present. Besides ornithine and urea, a product (or products) of yet unknown structure is formed in addition -especially under aerobic conditions. This activi ty remained associated with photosystem II complexes even after substantial additional treat ments to remove loosely bound proteins. On chlorophyll basis the maximal activity obtained under optimal assay conditions corresponded to 94 (miol ornithine formed/mg chloro phyll x h. This PS II associated, L-arginine metabolizing enzyme was isolated (utilizing a m an ganese charged chelating Sepharose 6 B column) and partially characterized. It could be shown that this enzyme requires manganese and chloride for its L-arginine metabolizing activity and that manganese becomes totally lost during purification indicating that manganese is bound to a fairly exposed site on the protein. Since it is rather unlikely that two different manganese and chloride binding proteins are present in such highly purified photosystem II complexes, the possibility of this protein being the water oxidizing enzyme will be discussed. W hether the manganese and chloride requiring L-arginine metabolizing activity of this protein which pro vided a suitable assay for its isolation from photosystem II complexes, has any physiological significance, can not be answered at the present time. | | | |
Reference
| Z. Naturforsch. 49c, 95—107 (1994); received July 13/September 25 1993 | | | |
Published
| 1994 | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0095.pdf | | | | Identifier
| ZNC-1994-49c-0095 | | | | Volume
| 49 | |
| 16 | Author
| G. H. Schmid, K. P. Bader, R. Schulder | Requires cookie* | | | Title
| A Study on the Life Time of the S3-State in the Filamentous Cyanobacterium Oscillatoria chalybea | | | | Abstract
| Filamentous Cyanobacterium, S-State, Metastable S3-State, Kok Model In the filamentous cyanobacterium Oscillatoria chalybea deactivation of the S-states start ing from steady-state conditions in which S0 = Sj = S2 = S3 = 25% reveals that S3 deactivates to a finite level of approx. 10%. This level is reached under normal conditions between 10-15 seconds. This quasi metastable S3 meets all requirements for S3 in that one flash eliminates this redox conditions to give S4 and therewith molecular oxygen. An analysis of the cyano-bacterial S-state system in the 5-state Kok model shows that the S-state population in the dark adapted sample contains no contribution from S_x or a more reduced condition which under normal conditions is the case for Chlorella or higher plant chloroplasts. Hence under standard conditions, the Oscillatoria condition is a pure Kok-4-condition in which S0 is the most reduced state. Under these conditions S2 seems to deactivate to Sv and S3 to S2 and to a smaller extent to S0. In the presence of the ADRY-reagent Ant-2-p (2-(3-chloro-4-tri-fluoromethyl)-anilino-3,5-dinitrothiophene) introduced by Renger (Biochim. Biophys. Acta 256,428,1972), which is supposed to specifically act on the S3-state (and thereby on S2), not only the deactivation kinetic of S3 (and S2) is accelerated (hence the life time of the S3-state is shortened), but also the level of metastable S3 becomes practically zero. An analysis of the deactivation pattern shows that the agent changes the mode of deactivation of the entire system. Thus, it is seen that after deactivation of a sample in presence of this agent the dark population of S-states contains the more reduced redox condition S_r It looks as if in this condition S2 deactivates not only to Sx but also to an appreciable extent by two steps to S_v Another agent ABDAC (alkyl-benzyl-dimethyl-ammoniumchloride) seems to lengthen the lifetime of the S2 and S3 condition in this cyanobacterium by apparently acting on the mem brane condition. | | | |
Reference
| Z. Naturforsch. 49c, 108—114 (1994); received July 26/October 111993 | | | |
Published
| 1994 | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0108.pdf | | | | Identifier
| ZNC-1994-49c-0108 | | | | Volume
| 49 | |
| 17 | Author
| O. Kruse, A. Radunz, G. H. Schmid | Requires cookie* | | | Title
| Phosphatidylglycerol and ß-Carotene Bound onto the D 1-Core Peptide of Photosystem II in the Filamentous Cyanobacterium Oscillatoria chalybea | | | | Abstract
| -particles from the cyanobacterium Oscillatoria chalybea were isolated by fractionating centrifugation. Purification of these particles was achieved by a 22 hours cen trifugation over a linear sucrose density gradient at 217.500 X g. The obtained particle frac tion exhibited an oxygen evolution activity which corresponded to three times the rate of intact cells and to five times the rate of intact thylakoids. The chlorophyll protein ratio was 1:10 and the ratio manganese/chlorophyll 1:34. SDS-polyacrylamide gel electrophoresis showed that the photosystem Il-fraction is com posed of the core peptides D 1 and D2, the chlorophyll-binding peptides CP 43 and CP 47, the extrinsic 33 kDa peptide (manganese stabilizing peptide, MSP) and phycobiliproteins with molecular masses between 16 to 20 kDa. Cyt b559 was not detected in our gel electro phoresis assay. Part of the peptides of the 30 kDa-region (D 1, D 2, MSP) occurred as aggre gates with a molecular mass of 60 to 66 kDa. The D 1-peptide was isolated from the PS Il-preparation by SDS-gel electrophoresis. The intrinisic peptide reacts in the Western blot procedure with the antiserum to phosphatidyl glycerol and with the antiserum to ß-carotene. Incubation of the peptide with the antisera to monogalactosyldiglyceride, sulfoquinovosyldiglyceride and zeaxanthine resulted negatively. The binding of phosphatidylglycerol onto the D 1-peptide was confirmed by lipid analysis in HPLC and fatty acid analysis by gas chromatography. Only this lipid, respectively the typi cal fatty acid mixture of this lipid was detected. The lipid is characterized by the fact that the hexadecenoic acid does not exhibit rraws-configuration, as is true for phosphatidylglycerol of higher plants and algae, but occurs in cw-configuration. With the antibody being directed towards the glycerol-phosphate residue and not towards the fatty acids, it can be concluded from the reaction of the antibodies with the bound lipid that the lipid is bound to the peptide via the fatty acid. The negatively charged phosphatidyl glycerol increases the hydrophobicity of the peptide and leads to a negatively charged sur face favouring binding of cations like calcium and magnesium. The fact that incubation of this PS Il-fraction with phospholipase inhibits photosynthetic activity by 25% which can be fully restored by addition of phosphatidylglycerol, shows that bound phosphatidylglycerol has a functional role. | | | |
Reference
| Z. Naturforsch. 49c, 115—124 (1994); received July 16/October 181993 | | | |
Published
| 1994 | | | |
Keywords
| D 1-Peptide, Phosphatidylglycerol, ß-Carotene, Antibody, Lipid-Protein Binding, Cyanobacterium, Manganese Stabilizing Peptide Photosystem II | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0115.pdf | | | | Identifier
| ZNC-1994-49c-0115 | | | | Volume
| 49 | |
| 18 | Author
| Fabrice Franck, M. Ohammed, Aziz Ouazzani, Esther Dujardin, Radovan Popovic | Requires cookie* | | | Title
| Optical Multichannel Analysis of Protochlorophyllide Phototransformation in Detergent-Solubilized Etioplast Membranes of Wheat | | | | Abstract
| Etioplast, Protochlorophyllide, Chlorophyllide, NADPH Extracts of wheat etioplast membranes obtained after treatment with 7 mM n-octyl-ß-D-glucopyranoside (OG), n-dodecyl-ß-D-maltoside (DM) or Triton X-100 contained the three spectral forms of Pchlide (the photoactive Pchlide638 and Pchlide650 and the inactive Pchlide630) in various relative amounts . The OG extract had a Pchlide composition close to that of the intact membranes whereas the DM extract was enriched in Pchlide638 and the Triton extract was enriched in Pchlide^,,. Measurements of the kinetics of phototransformation and of time-resolved absorbance spectra during phototransformation in continuous light shows that the inactive Pchlide^ is in fact slowly transformed to Chlide, especially in the Triton extract where this form is more abundant. Addition of NADPH favours the phototransformation of Pchlide630 and the slow regeneration of Pchlide638 and Pchlide650 from Pchlide630 in darkness after illumination. No such regeneration was however observed in the Triton extract. NADPH had only slight effects on the Chlide shift towards shorter wavelengths after phototransfor mation in solubilized membranes. | | | |
Reference
| Z. Naturforsch. 49c, 125—131 (1994); received June 71993 | | | |
Published
| 1994 | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0125.pdf | | | | Identifier
| ZNC-1994-49c-0125 | | | | Volume
| 49 | |
| 19 | Author
| Kirsten Lorenzen, Timm Anke, Uwe Anders, H. Erm An Hindermayr, Fritz Hansske | Requires cookie* | | | Title
| Two Inhibitors of Platelet Aggregation from a Panus Species (Basidiomycetes) | | | | Abstract
| Two inhibitors of platelet aggregation were isolated from fermentations of Panus sp. 9096. One inhibitor proved to be identical to naematolon (2), an antibiotic previously isolated by S. Backens et al. from several Hypholoma species. The other metabolite, panudial (1), is a new nordrimane (cw-annelation of the bicyclus) lacking the carbon atom in position 10 of the drimane skeleton. Panudial is a potent inhibitor of bovine and human platelet aggregation stimulated by different inducers. | | | |
Reference
| Z. Naturforsch. 49c, 132—138 (1994); received September 1/ | | | |
Published
| 1994 | | | |
Keywords
| Basidiomycetes, Lentineae, Panus Species, Platelet Aggregation, Antibiotics, Drimanes | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0132.pdf | | | | Identifier
| ZNC-1994-49c-0132 | | | | Volume
| 49 | |
|
