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  • 1
    Electronic Resource
    Electronic Resource
    Dissociation of bovine and bacterial catalases by sodium n-dodecyl sulfate (1982)
    New York : Wiley-Blackwell
    Biopolymers 21 (1982), S. 1435-1450 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The dissociation of beef liver and bacterial (Micrococcus lysodeikticus) catalases by the action of sodium n-dodecyl sulfate (SDS) has been investigated as a function of SDS concetration and time by ultracentrifugation. The rate of dissociation of beef liver catalase is found to be much faster than that for bacterial catalase in 25 mM SDS at pH 7.0. Beef liver catalase is dissociated into its four subunits after 24 h, whereas bacterial catalase is not completely dissociated after 36 days of incubation. The binding of SDS to beef liver catalase obeys a Hill equation with a cooperativity exponent of 2.0 and a binding constant of 440. The initial interaction of SDS with beef liver catalase can be detected by microcalorimetry, whereas the mixing of SDS with bacterial catalase is athermal. Bacterial catalase retains enzymic activity in the presence of SDS, whereas beef liver catalase is completely deactivated at SDS concentrations above 5 mM. Beef liver catalase is more sensitive to acid denaturation than bacterial catalase, and the rate of dissociation for both catalases is sixth-order in proton concentration. Comparison of the amino acid analysis of the two catalases shows that bacterial catalase has a smaller number of lysyl residues and a larger number of glutamyl residues than beef liver catalase. Taken together these structural differences could lead to a reduced affinity of bacterial catalase for the binding of SDS as observed.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360210712
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  • 2
    Electronic Resource
    Electronic Resource
    Quantitative XPS: The calibration of spectrometer intensity - energy response functions. 2 - Results of interlaboratory measurements for commercial instrumentsPaper presented at the Third International Conference on Quantitative Surface Analysis held at the National Physical Laboratory, Teddington, UK, 22-24 November 1983. (1984)
    Chichester [u.a.] : Wiley-Blackwell
    Surface and Interface Analysis 6 (1984), S. 242-254 
    Details
    ISSN: 0142-2421
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: An interlaboratory experiment to establish X-ray photoelectron spectrometer intensity-energy response functions has been completed. The measurements made by fifteen participants give results for seven instrument models from four manufacturers. Two methods of determining the response function are tested: (i) by peak area measurement and (ii) using the background data from wide scan spectra from reference foils of Cu, Ag and Au. The peak area data show excellent reproducibility, and area ratios, when corrected for instrument response functions, are consistent to a standard deviation of 4% for Ag and Au between all instruments and conditions. The response functions relative to the VG Scientific ESCA 3 Mk II are proportional to En where, in the constant ΔE mode, n = -;0.20±0.03 for the Leybold LHS10, -0.15±0.10 for the Perkin-Elmer PHI 550, 0.00±0.03 for the VG Scientific ESCA 3, and 0.20±0.02 for the VG Scientific ESCALAB I and II. The AEI/Kratos ES 200B/300 gives a complex, but defined, function. In the constant ΔE/E mode the latter instrument gives n in the range 1.3 to 2.0 and the VG Scientific ESCALAB II 1.79±0.05.
    Additional Material: 26 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/sia.740060507
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  • 3
    Electronic Resource
    Electronic Resource
    Detection of specific bovine serum albumin-sodium n-dodecyl sulphate complexes by polyacrylamide gel electrophoresis (1982)
    Weinheim : Wiley-Blackwell
    Electrophoresis 3 (1982), S. 317-321 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Polyacrylamide gel electrophoresis has been adapted to investigate bovine serum albumin (BSA) at sub-saturation concentration levels of sodium n-dodecyl sulphate (SDS). Two specific complexes were detected which coexisted between SDS concentrations of 0.4 and 5 mM. The binding isotherm for SDS on BSA was determined under comparable conditions by equilibrium dialysis and used in conjunction with the electrophoretic data to determine the composition of the complexes. The complexes had the following stoichiometry, BSA (SDS)5 and BSA (SDS)36, and closely resembled two of the three complexes that have been observed by moving boundary electrophoresis. The experiments indicate that the polyacrylamide gel electrophoresis (PAGE) technique when applied below surfactant saturation could be a useful tool in the study of protein-surfactant interactions.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150030604
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