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  • 1970-1974  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Über die Heterogenität der Aldolasen. Vorläufige MitteilungEine ausführliche Mitteilung ist im Europ. J. Biochemistry vorgesehen.. 17. Mitteilung über Aldolasen [1] (1970)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 53 (1970), S. 654-658 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Aldolase A (rabbit muscle) and aldolase B (human liver) have been resolved by isoelectric focusing into five distinct enzymatically active compounds. Each single component, if refocused under the same conditions, yields one single peak at the same isoelectric position as in the previous run. If component I or III are rehybridized (method of Penhoet et al.) component I yields one single peak, whereas component III yields the complete five membered set.Apparently the aldolases A and B are both tetrameres of two heterogeneous types of subunits α/α′ and β/β′ respectively. Analogous to the five membered set produced by hybridization of the aldolases A, B and C, the subunits α/α′ or β/β′, respectively, combine randomly to tetrameres forming five membered sets of the type α4, α3α′, α2α2′, α1α3′, α4′, etc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19700530326
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  • 2
    Electronic Resource
    Electronic Resource
    Heterogenität der Drosophila-Aldolase und Hybridisierung mit Säugeraldolase 20. Arbeit über aldolasen19. Arbeit über Aldolasen: S. [1]. (1971)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 54 (1971), S. 2809-2820 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: -1. FDP aldolase from pupae of Drosophila melanogaster is shown by the following findings to be a tetrameric molecule with two non-identical subunits: (a) Disc electrophoresis on polyacrylamide gel in the presence of sodium dodecylsulfate yields a subunit molecular weight of 40000 (equal to that of rabbit muscle aldolase). (b) Hybridisations of drosophila aldolase with type C aldolase from rabbit and calf brain lead to a five-membered set of isoenzymes.2. The non-identity of the subunits is suggested by the behaviour on isoelectro focussing. While rabbit muscle aldolase and human liver aldolase show five isoenzymes (hybrids from the non-identical subunits), drosophila aldolase can be separated into three peaks only. This result may be interpreted in two ways: (a) The isoenzymes α4 and α3α′ are not separated from each other in the pH range 5--8, neither are αα′3 and α′4. Or (b) α2 and α′2 are not split under the condition of isoelectro focussing and therefore 3 isoenzymes α4, α2α′2, and α′4 are obtained only.(3) Isoenzyme I (supposedly mainly α4) and isoenzyme III (supposedly mainly α′4) are identical in the following respects: Michaelis constant, pH profile, FDP/F-1-P activity ratio, inactivation by carboxypeptidase A, disc electrophoresis on polaycrylamide and molecular weight. The only difference found between isoenzyme I and III is the specific activity: Isoenzyme I is nearly twice as active as isoenzyme III.4. The fact that hybridisation between drosophila aldolase and type C aldolase from rabbit and calf brain yields a set of isoenzymes proves that interspecies hybridisation is possible between FDP aldolases from vertebrates and invertebrates. FDP aldolases from vertebrates and invertebrates seem to be homologous enzymes. Our results suggest that the conformation of aldolases remained relatively unchanged during evolution.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19710540848
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  • 3
    Electronic Resource
    Electronic Resource
    Die Stereospezifität der Alkoholdehydrogenase (1970)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 53 (1970), S. 732-738 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The glyceraldehyde formed by oxidation of glycerol through alcohol dehydrogenase (E.C. 1.1.1.1) from horse liver has been condensed with phosphodihydroxyacetone using either rabbit muscle or liver aldolase. The single product was identified after silylation by gas chromatography as L-sorbose-1-phosphate. No D-fructose-1-phosphate was detected. Apparently liver alcohol dehydrogenase oxidizes glycerol stereospecifically to L-(-)-glyceraldehyde. Thus, the earlier conclusions of Hadorn et al. from chromatography of the borate complexes on Dowex 1 have been confirmed. The same stereospecific behavior was found for both isoenzymes III and IV.With Bis-(trimethylsilyl)-trifluoroacetamide L-sorbose-1-phosphate and D-fructose-1-phosphate are persilylated. Two trimethylsilyl groups are bound to the phosphate group. These bonds are not cleaved during gas chromatography.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19700530406
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    Paper (German National Licenses)
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