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  • 1
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 672 (1992), S. 0 
    ISSN: 1749-6632
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Allgemeine Naturwissenschaft
    Notizen: The relationship between enzyme hydration and the catalytic activity of chymo-trypsin powders suspended in nearly anhydrous 1 M n-propanol/toluene solutions has been studied. The enzyme hydration range examined extends from approximately 2 to 10 wt% water sorbed. Measurements of apparent enzyme activity and the number of active sites as a function of enzyme hydration were used to calculate intrinsic enzyme activity as a function of enzyme hydration. It was found that the apparent enzyme activity increased linearly over this hydration range and that approximately 30% of the enzyme was catalytically active independent of the hydration level. Thus, the observed increase in apparent catalytic activity with increasing enzyme hydration results from an increase in the catalytic efficiency of a fixed number of active sites, rather than an increase in the population of active sites. Inhibitor binding in the organic suspension was also measured using the transition state analogue, (R)-1-acetamido-2-phenylethane boronic acid, which binds reversibly to the active site of the enzyme. The inhibition results suggest that one role of water in activating nearly dry enzyme suspensions is to enhance the intrinsic catalytic activity through transition state stabilization.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    s.l. : American Chemical Society
    Macromolecules 28 (1995), S. 5655-5663 
    ISSN: 1520-5835
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    ISSN: 1520-5835
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    New York : Wiley-Blackwell
    Biopolymers 33 (1993), S. 1213-1224 
    ISSN: 0006-3525
    Schlagwort(e): Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Water sorption isotherms at 27°C have been measured for lysozyme and chymotrypsin in suspensions of toluene, di(n-butyl) ether, n-propanol, and a solution of 1M n-propanol in benzene. Sorption isotherms for the different suspensions are compared by converting solvent water content to the thermodynamic activity of water in each solvent. The sorption behavior is also compared to that for the two proteins hydrated from the vapor phase. At low water activities, all sorption isotherms are similar when compared on the basis of water activity. However, at higher activities, water sorption by the proteins in the organic suspensions is suppressed relative to the sorption of water vapor. The greatest suppression is observed for n -propanol, which suggests that the suppression may be due to a competition for water-binding sites on the protein by the organic solvent. Sorption isotherms at low water activities have also been predicted using a thermodynamic model in which it is assumed that water binds selectively to the ionizable residues on the surface of the protein. A comparison of predicted and measured sorption isotherms shows that the model can provide reasonable estimates of water sorption in nonpolar or moderately polar organic solvent suspensions at low levels of hydration. © 1993 John Wiley & Sons, Inc.
    Zusätzliches Material: 10 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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