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  • Artikel  (18)
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  • Springer  (18)
  • American Chemical Society (ACS)
  • Elsevier
  • Frontiers Media
  • Oxford University Press
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  • 2015-2019
  • 1995-1999
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  • 1
    Digitale Medien
    Digitale Medien
    Kinetics of the appearance of mRNA for light-harvesting chlorophyll a/b protein in polysomes of barley (1980)
    Springer
    Planta 148 (1980), S. 448-452 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Chlorophyll protein ; Hordeum ; Photosynthesis (light harvesting) ; Poly(A)RNA ; Polysomes ; Thylakoid membranes
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Polysomes from dark-grown and illuminated barley seedlings were translated in cell-free systems. The translation products reacting with the antibody against the light-harvesting chlorophyll a/b protein (LHCP) were analyzed by polyacrylamide gel electrophoresis. It was found that, in addition to the precursor protein of LHCP, a product was obtained that co-migrated with the mature protein. Furthermore, the results show that the light-induced proly(A)RNA for LHCP is integrated into the polysomal complex without delay, indicating that the integration of LHCP into the membrane is controlled at a higher level of gene expression.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02395313
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    The effect of differential root and shoot temperature on the nitrate reductase activity, assayed in vivo and in vitro in roots ofHordeum vulgare (barley) (1980)
    Springer
    Planta 148 (1980), S. 455-461 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Carbohydrates (in roots) ; Hordeum ; Malate ; Nitrate reductase activity ; Temperature (and nitrate reductase activity)
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract There was a large increase in nitrate reductase activity (NAR) assayed both in vivo and in vitro in roots of barley plants (cv. Midas_ grown with roots at 10°C and shoots at 20°C, compared with whole plants grown at 20°C. There were diurnal fluctuations in NRA in roots from both treatments, but they were much greater in roots grown at 20°C, where NRA fell to a very low value in the dark period. The diurnal fluctuations in the malate content of the roots were also related to the root growth temperature. Plants with roots grown at the lower temperature had a higher malate content, especially in the dark period where it was 20 times greater than in plants with roots at 20°C. At all times there was a three-fold increase in soluble carbohydrate in cooled roots and diurnal fluctuations were much less pronounced than those of malate. Growth at low temperatures increased the total flux of amino N into the xylem sap and increased the proportion of reduced N in the total N flux. At certain times of day both 10°C- and 20°C-grown roots responded to exogeneous malate by increasing the flux of amino acid into the xylem sap, although this effect was always more pronounced in 20°C-grown roots.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02395315
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Mobilization of proline in the starchy endosperm of germinating barley grain (1980)
    Springer
    Planta 149 (1980), S. 149-154 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Endosperm ; Germination (seeds) ; Hordeum ; Proline ; Reserve mobilization (seeds) ; Seed germination
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract In germinating grains of barley, Hordeum vulgare L. cv. Himalaya, free proline accumulated in the starchy endosperm during the period of rapid mobilization of reserve proteins. When starchy endosperms were separated from germinating grains and homogenized in a dilute buffer of pH 5 (the pH of the starchy endosperm), the liberation of proline continued in these suspensions. The process was completely inhibited by diisopropylfluorophosphate, indicating that it was totally dependent on serine carboxy-peptidases. The carboxypeptidases present in the starchy endosperms of germinating grains were fractionated by chromatography on DEAE-cellulose. Four peaks were obtained, all with different activity spectra on the seven carbobenzoxydipeptides (Z-dipeptides) tested. Two of the peaks corresponded to previously known barley carboxypeptidases; these as well as a third peak hydrolyzed substrates of the types Z-X-Y and Z-X-Pro (X and Y denote any amino acid residue except proline). The fourth peak corresponded to a proline carboxypeptidase specific for substrates of the Z-Pro-X type. Apparently, in the hydrolysis of longer proline-containing peptides there must be sequential cooperation between the two carboxypeptidase types. The carboxypeptidases in extracts of starchy endosperms also liberated proline from the peptides Ala-Ala-Ala-Pro and Ala-Ala-Pro while Ala-Pro and Pro-Ala were not attacked. The dipeptides, however, were rapidly hydrolyzed around pH 7 by extracts prepared from the scutella of germinating grains. It is concluded that one part of the proline residues of the reserve proteins is liberated in situ in the starchy endosperm through the combined action of acid proteinases and carboxypeptidases, while another part is taken up in the form of small peptides by the scutellum, where proline is liberated by amino- and/or dipeptidases in some “neutral compartment”.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00380876
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Nature of the phytochrome effect on the binding of glycolate oxidase to peroxisomes in vitro (1980)
    Springer
    Planta 149 (1980), S. 252-256 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Glycolate oxidase ; Hordeum ; Phytochrome ; Peroxisomes
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The attachment of glycolate oxidase to the peroxisomal fraction derived from etiolated barley leaves (Hordeum vulgare L. cr. Dvir) is affected by light. The effect of red irradiation is reversed by subsequent far-red irradiation, indicating the involvement of phytochrome. This phytochrome effect is assumed to be related to phytochrome binding. Indeed, prevention by filipin (1.2·10-6 mol g-1 f wt) or cholesterol of phytochrome binding to membranes abolishes the effect of light on the interaction between glycolate oxidase and the peroxisomal fraction. Glycolate oxidase binding is affected by addition of quasi-ionophores such as gramicidin and filipin at a concentration of 0.6·10-3 mol g-1 f wt. This fact indicates that peroxisome-glycolate oxidase interaction may be affected by membrane potential. Since both ion transport and membrane potential are known to be affected by phytochrome, it is proposed that phytochrome acts in the light-induced modulation of glycolate oxidase attachment as a quasi-ionophore.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00384561
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
    Digitale Medien
    Digitale Medien
    In vitro synthesis of barley storage proteins (1980)
    Springer
    Planta 149 (1980), S. 262-268 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Hordeum ; Polyribosomes ; Protein synthesis ; RNA ; Seeds ; Storage proteins
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Membrane-bound polysomes were isolated from developing endosperms of barley (Hordeum vulgare L.) and shown to support the synthesis of trichloroacetic acid-insoluble material by an in vitro wheat germ protein synthesis system. The mRNA associated with the polysomes was separated from the ribosomes by affinity chromatography on oligo-dT cellulose and was also shown to support in vitro protein synthesis. The poly-A+ RNA isolated contained material of between 0.55 and 2.55 kilobases in length with about 6% poly A. The products of in vitro protein synthesis resembled hordeins (the prolamin storage proteins of the barley endosperm) in that they were predominantly soluble in 55% propan-2-ol, contained a low proportion of lysine as compared with leucine and had similar, but not identical, electrophoretic properties. The differences in the electrophoretic behaviour between the products of poly-A+ RNA translation and authentic hordeins is suggested to be due to the presence of an extra (leader?) sequence on the former.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00384563
    Standort Signatur Erwartet Verfügbarkeit
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  • 6
    Digitale Medien
    Digitale Medien
    Differential expression of the genes for ribulose-1,5-bisphosphate carboxylase and light-harvesting chlorophyll a/b protein in the developing barley leaf (1980)
    Springer
    Planta 150 (1980), S. 41-45 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Chlorophyll-protein ; Hordeum ; Leaf development ; Light-harvesting chlorophyll a/b protein ; mRNA ; Ribulose-1,5-bisphosphate carboxylase
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The expression of genes in particular for light-harvesting chlorophyll a/b protein (LHCP) and ribulose-1,5-bisphosphate carboxylase (RuBPCase) has been studied in the developing barley leaf. This has been done by analysis of the occurrence of both proteins within the different regions (1 to 6, beginning from the base) of the primary 7-day-old leaf. It has been found that LHCP already appears in the base of the leaf, whereas RuBPCase is primarily expressed in the apical expanding part of the leaf. The distribution of the mRNAs for both proteins within this gradient is in accordance with that of the proteins themselves, indicating that gene expression is not regulated at the level of translation in both cases. The poly(A) mRNA for LHCP occurs mainly in the basic sections 2 and 3, whereas that for RuBPCase is found throughout the leaf but primarily in the apical sections of the leaf.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00385613
    Standort Signatur Erwartet Verfügbarkeit
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  • 7
    Digitale Medien
    Digitale Medien
    Light-induced changes in the amounts of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase and its mRNA in barley plants grown under a diurnal light/dark cycle (1987)
    Springer
    Planta 170 (1987), S. 453-460 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Hordeum ; NADPH-protochlorophyllide oxidoreductase ; Polypeptide (amount, light-induced changes)
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Seedlings of barley were grown either in continuous darkness or under a diurnal 12 h light/12 h dark cycle and the effects on NADPH-protochlorophyllide oxidoreductase were followed at two different levels. Firstly, the relative content of the mRNA encoding the NADPH-protochlorophyllide oxidoreductase was measured by dot-blot hybridization. Secondly, changes in the enzyme polypeptide were monitored either by the method of immunoblotting or by immunogold labelling of ultrathin sections of Lowicryl-embedded leaf tissue. Our results demonstrate that drastic diurnal changes in the level of mRNA sequences and the enzyme protein are unlikely to occur in plants which have been grown under natural light/dark conditions. In the dark, protein and mRNA accumulation occurs at an early developmental stage. These results are difficult to reconcile with the suggestion that the massive accumulation of mRNA and enzyme protein in dark-grown seedlings is primarily the consequence of an artificially extended darkperiod. In addition to the plastid-specific NADPH-protochlorophyllide oxidoreductase a closely related polypeptide has been detected outside the plastid in the surrounding cytoplasm (Dehseh et al. 1986b, Planta 169, 172–183). During the diurnal light/dark treatment of seedlings the concentrations of the two protein populations did not show any variation indicative of an exchange between the two protein populations across the plastid envelope.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00402979
    Standort Signatur Erwartet Verfügbarkeit
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  • 8
    Digitale Medien
    Digitale Medien
    The effect of differential root and shoot temperature on the nitrate reductase activity, assayed in vivo and in vitro in roots ofHordeum vulgare (barley) (1980)
    Springer
    Planta 148 (1980), S. 455-461 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Carbohydrates (in roots) ; Hordeum ; Malate ; Nitrate reductase activity ; Temperature (and nitrate reductase activity)
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract There was a large increase in nitrate reductase activity (NAR) assayed both in vivo and in vitro in roots of barley plants (cv. Midas_ grown with roots at 10°C and shoots at 20°C, compared with whole plants grown at 20°C. There were diurnal fluctuations in NRA in roots from both treatments, but they were much greater in roots grown at 20°C, where NRA fell to a very low value in the dark period. The diurnal fluctuations in the malate content of the roots were also related to the root growth temperature. Plants with roots grown at the lower temperature had a higher malate content, especially in the dark period where it was 20 times greater than in plants with roots at 20°C. At all times there was a three-fold increase in soluble carbohydrate in cooled roots and diurnal fluctuations were much less pronounced than those of malate. Growth at low temperatures increased the total flux of amino N into the xylem sap and increased the proportion of reduced N in the total N flux. At certain times of day both 10°C- and 20°C-grown roots responded to exogeneous malate by increasing the flux of amino acid into the xylem sap, although this effect was always more pronounced in 20°C-grown roots.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00552660
    Standort Signatur Erwartet Verfügbarkeit
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  • 9
    Digitale Medien
    Digitale Medien
    The isolation of endoplasmic reticulum from barley aleurone layers (1980)
    Springer
    Planta 150 (1980), S. 58-69 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Aleurone ; α-Amylase ; Endoplasmic reticulum ; Hordeum ; Organelle isolation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Techniques for the isolation and purification of endoplasmic reticulum (ER) from aleurone layers of barley (Hordeum vulgare L.) were assessed. Neither differential centrifugation nor density gradient centrifugation of a homogenate separate the ER or other organelles of this tissue from the lipidcontaining spherosomes. Isopycnic sucrose gradient centrifugation of organelles first purified by molecular sieve chromatography on Sepharose 4B, however, results in separation of the organelles based on their differing buoyant densities. Manipulation of the magnesium concentration of the isolation media and density-gradient solutions affords isolation of ER at a density of 1.13–1.14 g cc-1 and 1.17–1.18 g cc-1. Electron microscopy shows that the membranes sedimenting at 1.13–1.14 g cc-1 are devoid of ribosomes and are characteristic of smooth ER, while those sedimenting at 1.17–1.18 g cc-1 are studded with ribosomes and have the features of rough ER. Endoplasmic reticulum isolated by isopycnic density gradient centrifugation can be further purified by rate-zonal centrifugation.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00385616
    Standort Signatur Erwartet Verfügbarkeit
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  • 10
    Digitale Medien
    Digitale Medien
    Quantitative and qualitative changes in the endoplasmic reticulum of barley aleurone layers (1980)
    Springer
    Planta 150 (1980), S. 70-81 
    Details
    ISSN: 1432-2048
    Schlagwort(e): Aleurone ; α-Amylase ; Endoplasmic reticulum ; Gibberellin ; Hordeum ; Organelle isolation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Changes in the level of the endoplasmicreticulum (ER) marker enzyme cytochrome-c reductase (EC 1.6.2.1) were followed with time of imbibition of de-embryonated half-seeds of barley (Hordeum vulgare L.) and the subsequent incubation of their aleurone layers in gibberellic acid (GA3) and H2O. During imbibition there is an increase in the level of cytochrome-c-reductase activity and in the amount of 280-nm absorbance associated with this enzyme. When aleurone layers are incubated for a further 42 h in water, there is a doubling of the cytochrome-c-reductase activity. In GA3, the activity of cytochrome-c reductase reaches a maximum at 24 h of incubation and thereafter falls to below 70% of its level at the beginning of the incubation period. Changes in the cytochrome-c-reductase activity correlate with changes in the fine structure of the aleurone cell. The ER isolated in low Mg2+ from aleurone layers incubated in buffer for up to 18 h has buoyant density of 1.13–1.14 g cc-1 while that from layers incubated in GA3 for 7.5–18 h has a density of 1.11–1.12 g cc-1. The α-amylase (EC3.2.1.1) isolated with the organelle fraction by Sepharose gel filtration is associated with the ER on isopycnic and rate-zonal density gradients, and its activity can be enhanced by Triton X-100. The soluble α-amylase fraction from Separose-4B columns, on the other hand, is not Triton-activated but is acid-labile. Acid phosphatase (EC3.1.3.2) is distributed in at least three peaks on isopycnic gradients. In low Mg2+ the second peak of activity has a density of 1.12 g cc-1 in GA3-treated tissue and 1.13–1.14 g cc-1 in H2O-treated tissue. With high-Mg2+ buffers, this peak of phosphatase activity disappears. Acid-phosphatase activity is not enhanced by Triton X-100 nor is it acid-labile.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00385617
    Standort Signatur Erwartet Verfügbarkeit
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