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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
    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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  • 3
    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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  • 4
    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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  • 5
    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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  • 6
    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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  • 7
    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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  • 8
    Electronic Resource
    Electronic Resource
    The control of glycolysis in aged slices of carrot root tissue (1974)
    Springer
    Planta 118 (1974), S. 211-224 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The possibility that the rate of glycolysis in aged slices of carrot (Daucus carota L.) is controlled by the enzyme phosphofructokinase was examined, by changing the rate of metabolism, by supplying the tissue with potassium chloride, potassium phosphate and potassium citrate and measuring the subsequent changes in levels of metabolites. Potassium chloride and potassium phosphate stimulate glycolysis, potassium citrate inhibits glycolysis and the associated changes in metabolites are consistent with the view that respiration is controlled by a dual system involving phosphofructokinase and glyceraldehyde phosphate dehydrogenase or possibly phosphoglycerate kinase. It is proposed that the control points are interlocked by phosphoenolpyruvate and phosphoglycerate. Thus if glyceraldehyde phosphate dehydrogenase is activated leading to an accumulation of phosphoglycerate and phosphoenolpyruvate, these compounds will inhibit phosphofructokinase. Thus our proposal for metabolic control in carrot resembles those proposed in mammalian systems except that the negative feedback system involving ATP and AMP which controls phosphofructokinase in mammals is replaced by a negative feedback system involving phosphoenolpyruvate and phosphoglycerate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00384777
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  • 9
    Electronic Resource
    Electronic Resource
    The control of NAD specific malic enzyme from cauliflower bud mitochondria by metabolites (1975)
    Springer
    Planta 126 (1975), S. 197-211 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary NAD malic enzyme (EC. 1.1.1.39) has been purified from cauliflower (Brassica oleracea. var. botrytis) bud mitochondria. The enzyme exhibits complex regulatory properties being activated by a variety of metabolites including glycolytic intermediates, CoA, sulphate and Krebs cycle acids—the tricarboxylic acids with the exception of citrate being more effective than dicarboxylic acids. Fructose diphosphate which is a positive effector of the enzyme increases the affinity of the enzyme for L-malate. The enzyme is inhibited by glutamate, aspartate, phosphate and ATP, in the latter case the inhibition is largely due to chelation of Mg2+. The plot of rate versus malate concentration is sigmoid at pH 7.0 with Mg2+ but normal Michaelis-Menten kinetics are observed with Mn2+. The molecular weight of the enzyme as measured by gel filtration is ca. 400000. The physiological significance of the responses to metabolites is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00388963
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  • 10
    Electronic Resource
    Electronic Resource
    The regulation of potato phosphoenolpyruvate carboxylase in relation to a metabolic pH-stat (1977)
    Springer
    Planta 133 (1977), S. 281-287 
    Details
    ISSN: 1432-2048
    Keywords: PEP carboxylase ; pH-stat ; Potato tuber ; Solanum tuberosum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Phosphoenolpyruvate (PEP) carboxylase (E.C. 4.1.1.31.) was extracted from potato tubers (Solanum tuberosum L.) and investigated for regulatory response to metabolites. The enzyme was found to be activated by sugar phosphates and glycollate and non-competitively inhibited by succinate and fumarate. In both cases the effects were highly dependent on pH, being maximal between pH 7 and 7.6. Rapid extraction techniques demonstrated that the enzyme suffers a sharp decline in activity and sensitivity to metabolites during the first 2 h from extraction. The observed properties of PEP carboxylase were related to the possible role of the enzyme in a metabolic pH-stat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00380690
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