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  • 1
    Electronic Resource
    Electronic Resource
    The Heat Capacity of Gaseous 1,3-Butadiene from 0 to 100° (1944)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 66 (1944), S. 2033-2035 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja01240a011
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  • 2
    Electronic Resource
    Electronic Resource
    The Central Role of Phosphoenolpyruvate in Plant Metabolism (1979)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology 30 (1979), S. 131-158 
    Details
    ISSN: 0066-4294
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.pp.30.060179.001023
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  • 3
    Electronic Resource
    Electronic Resource
    The fine control of cytosolic pH (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 67 (1986), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1986.tb05081.x
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  • 4
    Electronic Resource
    Electronic Resource
    Formation of Phosphoserine from 3-Phosphoglycerate in Higher Plants (1958)
    [s.l.] : Nature Publishing Group
    Nature 182 (1958), S. 532-533 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] D-3-Phosphoglycerate-32P was prepared by a modification of the method of Neuberg and Lustig7. The purity of the compound was established by chromatography and the chromatographically pure compound was eluted from the paper. The enzyme system was prepared from 8-10 day old pea epicotyls (110 gm.) ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/182532a0
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  • 5
    Electronic Resource
    Electronic Resource
    Synthesis of Succinate from Acetate by an Enzyme System of Pig Heart Muscle (1958)
    [s.l.] : Nature Publishing Group
    Nature 181 (1958), S. 339-340 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] This report presents evidence that an enzyme system present in pig heart muscle catalyses the oxidation and condensation of acetate to form succinate. The enzyme was prepared by extracting an acetone-dried powder of pig heart muscle with potassium phosphate buffer (0-1 M, pH. 7-4) and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/181339a0
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  • 6
    Electronic Resource
    Electronic Resource
    Synthesis of Succinate from Acetate (1961)
    [s.l.] : Nature Publishing Group
    Nature 191 (1961), S. 1093-1093 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] This explanation has been tested by attempting to measure the formation of acetate-14C from suc-cinate-2.3-14C with preparations capable of incorporating acetate-14C into succinate. Such experiments failed to demonstrate any significant formation of acetate, acetyl co-enzyme A or acetyl phosphate ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/1911093a0
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  • 7
    Electronic Resource
    Electronic Resource
    Aromatische Biosynthese in höheren Pflanzen. 1. Darstellung und Eigenschaften von Dehydroshikimsäure-Reductase (1962)
    Springer
    Colloid & polymer science 183 (1962), S. 84-84 
    Details
    ISSN: 1435-1536
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02260562
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  • 8
    Electronic Resource
    Electronic Resource
    Serine–Glycine Interconversion in Plant Tissues (1958)
    [s.l.] : Nature Publishing Group
    Nature 181 (1958), S. 1070-1071 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] That the interconversion occurred in plant tissues seemed probable in view of labelling data obtained by Tolbert and Cohan4, who fed 1-14C- or 2-14C-labelled glycollate to wheat and barley leaves and found, in short experiments, that serine and glycine were the only major products labelled. The 2-C ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/1811070a0
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  • 9
    Electronic Resource
    Electronic Resource
    The physiological role of the isoenzymes of lactate dehydrogenase in potatoes (1984)
    Springer
    Planta 161 (1984), S. 272-280 
    Details
    ISSN: 1432-2048
    Keywords: Isoenzyme ; Lactate dehydrogenase (isoenzymes) ; Solanum (lactate dehydrogenase)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Four of the five isoenzymes of lactate dehydrogenase present in potato tubers have been isolated and their kinetic properties examined. The pyruvate-reductase activity of isoenzyme-4 is greatly reduced at low pH, the affinity for both pyruvate and NADH is reduced and ATP has a stronger inhibitory effect. If the design properties of an enzyme dictate a high affinity for substrates, then the Km values for lactate, glyoxylate and NAD are consistent with an oxidative role for isoenzyme-4. The same considerations do not permit a conclusion about the physiological role of isoenzymes-1 to-3. However, an overview of the kinetic properties of these isoenzymes indicates that isoenzyme-1 is best adapted for the role of pyruvate reductase. Consideration of the relationships between kinetic constants and electrophoretic mobilities of the isoenzymes, leads us to predict that isoenzyme-5 is well adapted for a role in the oxidation of lactate or glyoxylate. The lactate dehydrogenase of potato leaves appears to consist prodominantly of an isoenzyme with the same mobility as isoenzyme-2 of the tubers and the two isoenzymes are probably identical. The kinetic properties of this isoenzyme are consistent with roles in either oxidation or reduction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00982925
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  • 10
    Electronic Resource
    Electronic Resource
    Protein turnover in the attached leaves of non-stressed and stressed barley seedlings (1982)
    Springer
    Planta 154 (1982), S. 435-440 
    Details
    ISSN: 1432-2048
    Keywords: Hordeum ; Leaf (protein) ; Protein turnover ; Water stress
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Protein turnover was examined, using tritiated water, in various 2-cm regions of 7-11-d-old, first leaves of barley (Hordeum vulgare). Differences were found between the regions in their protein turnover and their responses to stress. The rate constant for degradation for total protein was the same throughout the leaf and the average half-life (t1/2) of protein=approx. 220 h. Only in the older regions did a 24-h pulse of3H2O preferentially label protein with a t1/2 (90 h) considerably shorter than the t1/2 for total protein. ‘Soluble’ protein was degraded faster than ‘insoluble’ protein and contained an appreciable short-lived protein component observable by short-pulse labelling. The rate of protein synthesis was greatest in the cells of the youngest region and declined as each region aged. The mean rate of protein synthesis over the 4-d period was 4 and 7 nmol h-1 of amino-N with respect to the regions 1–3 and 7–9 cm from the leaf tip. Seedlings, stressed by adding polyethylene glycol (2.0 MPa) to the roots, showed a marked loss of protein from the older leaf regions with only small losses in the younger regions. Amino acids accumulated in the younger region continuously whereas in the older region little accumulation occurred until day 3 of stress when proline levels increased. Protein synthesis was decreased by between 30% and 50% in all leaf regions. In the region 1–3 cm from the leaf tip, the rate of protein degradation of total protein was enhanced and equalled the rate of degradation of 24-h-pulse-labelled protein which was not itself significantly affected by stress (t1/2=approx. 90 h). In the region 3–5 cm, the degradation of both 4-d and 24-h-labelled protein was enhanced by stress to rates similar to those found in the region 1–3 cm. This was largely through increases in the degradation of the ‘insoluble’ protein, but the degradation of ‘soluble’ protein was also raised. Protein degradation in the region 7–9 cm was not affected by stress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01267810
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