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  • (human)  (1)
  • 1D trNOESY-TOCSY  (1)
  • Springer  (2)
  • American Institute of Physics
  • Copernicus
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  • Springer  (2)
  • American Institute of Physics
  • Copernicus
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  • 1
    Electronic Resource
    Electronic Resource
    Enzymatic properties of overexpressed human hexokinase fragments (1998)
    Springer
    Molecular and cellular biochemistry 189 (1998), S. 185-193 
    Details
    ISSN: 1573-4919
    Keywords: recombinant hexokinase domains ; kinetic properties ; (human)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Full-length hexokinase (HK; ATP: D-hexose 6-phosphotransferase, EC 2.7.1.1), a truncate form of the enzyme lacking the first 11 amino acids (HK-11aa) and the 50 kDa C-terminal half (‘mini’-HK) containing the catalytic domain, were overexpressed and purified to homogeneity to investigate the influence of the N-terminal region of human hexokinase type I (HK) on its regulatory properties. All forms of the enzyme are catalytically active with the HK-11aa being the most active. All the forms of HK showed the same affinity for glucose and MgATP and were also inhibited by glucose 6-phosphate (Glc 6-P) competitively vs. MgATP with similar Kis (28.5-37 μM). Glucose 1,6-bisphosphate (Glc 1,6-P2) was also a strong inhibitor of all HKs without significant differences among the different truncate forms of the enzyme (Kis 49.5-59 μM). At low concentrations (0-3 mM), Pi was able to reverse the sugar phosphate inhibition of the full-length HK and HK-11aa but not of the ‘mini’-HK. In contrast, at high concentrations Pi was an inhibitor of all the hexokinases investigated. These findings confirm that Pi has a low affinity binding site on the C-terminal of HK while counteracts glucose 6-phosphate inhibition by binding to or requiring the N-terminal half of the enzyme. The first 11 N-terminal amino acids influence the specific activity of HK but are unable to affect the kinetic properties investigated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006962217495
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  • 2
    Electronic Resource
    Electronic Resource
    Application of homonuclear 3D NMR experiments and 1D analogs to study the conformation of sialyl Lewisx bound to E-selectin (1997)
    Springer
    Journal of biomolecular NMR 9 (1997), S. 423-436 
    Details
    ISSN: 1573-5001
    Keywords: 3D TOCSY-trNOESY ; 1D TOCSY-trNOESY ; 1D trNOESY-TOCSY ; trNOE ; trROE ; E-selectin ; sialyl Lewisx
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The conformation of the sialyl Lewis x tetrasaccharidebound to E-selectin was previously determined from transfer NOE (trNOE)experiments in conjunction with a distance-geometry analysis. However, theorientation of the tetrasaccharide ligand in the binding site of E-selectinis still unknown. It can be predicted that the accurate quantitativeanalysis of all trNOEs, including those originating from spin diffusion, isone key to analyze the orientation of sialyl Lewisx in thebinding pocket of E-selectin. Therefore, we applied homonuclear 3D NMRexperiments and 1D analogs to obtain trNOEs that could not unambiguously beassigned from previous 2D trNOESY spectra, due to severe resonance-signaloverlap. A 3D TOCSY-trNOESY experiment, a 1D TOCSY-trNOESY experiment, and a1D trNOESY-TOCSY experiment of the sialyl Lewisx/E-selectincomplex furnished new interglycosidic trNOEs and provided additionalinformation for the interpretation of trNOEs that have been describedbefore. A 2D trROESY spectrum of the sialyl Lewisx/E-selectincomplex allowed one to identify the amount of spin-diffusion contributionsto trNOEs. Finally, an unambiguous assignment of all trNOEs, and an analysisof spin-diffusion pathways, was obtained, creating a basis for aquantitative analysis of trNOEs in the sialylLewisx/E-selectin complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018358929268
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