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  • 1
    Electronic Resource
    Electronic Resource
    Encapsulation of the ferritin protein in sol-gel derived silica glasses (1996)
    Springer
    Journal of sol gel science and technology 7 (1996), S. 109-116 
    Details
    ISSN: 1573-4846
    Keywords: ferritin ; sol-gel ; magnetism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A significant recent development in sol-gel science has been the encapsulation of biomolecules such as proteins and enzymes in optically transparent silica glasses. This paper reports on the encapsulation of an iron (Fe) storage protein, ferritin, to develop a magnetic silica glass. Native ferritin, which has a nanometer-sized microcrystalline Fe oxide core, was encapsulated in optically transparent silica glasses using the sol-gel process. Fe could be released from ferritin but could not be reconstituted into apoferritin when the protein was trapped in the pores of the glass. Transmission electron microscopy of ferritin-doped aged silica gels indicated that crystallinity of the Fe oxide core was retained upon sol-gel encapsulation. Magnetic measurements on ferritin-doped silica gels indicated the material to be paramagnetic, but not superparamagnetic.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00401890
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  • 2
    Electronic Resource
    Electronic Resource
    Spectroscopic determination of cholinesterase activity and inhibition in sol-gel media (1997)
    Springer
    Journal of sol gel science and technology 8 (1997), S. 1067-1070 
    Details
    ISSN: 1573-4846
    Keywords: cholinesterase ; sol-gel ; pesticide ; THA ; enzyme activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Biological activity of cholinesterases can be determined by optically monitoring the enzymatic reaction with indophenyl acetate, (N-4′-acetoxyphenyl)-4-quinone imine. At pH 8.0 cholinesterases hydrolyze this yellow dye to yield a blue reaction product. Cholinesterase inhibitors reduce the rate of this hydrolysis. Thus, by monitoring absorbance of the hydrolysis product at its maximum (630 nm) as a function of time, reaction rates of both cholinesterase activity and cholinesterase inhibition may be quantified spectroscopically. Using this technique, we measured the enzymatic activity of butyrylcholinesterase (BuChE) molecules encapsulated in tetramethyl orthosilicate (TMOS) silicate gel-glass prepared by hydrolysis and condensation. This activity is reduced, in a concentration-dependent manner, by the reversible cholinesterase inhibitors 1,5-bis(4-allyldimethyl-ammoniumphenyl) pentan 3-one dibromide (BADAPP) and 9-amino-1,2,3,4-tetrahydroacridine (THA; tacrine, Cognex). The gel-glasses are rigid, and compact, transparent and porous enough to allow reagents to diffuse in and out.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02436985
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  • 3
    Electronic Resource
    Electronic Resource
    Allosteric Regulation of Enzymatic Reactions in a Transparent Inorganic Sol-Gel Material (1999)
    Springer
    Journal of sol gel science and technology 15 (1999), S. 57-62 
    Details
    ISSN: 1573-4846
    Keywords: glutamate dehydrogenase ; allosteric regulators ; sol-gel ; enzyme activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Glutamate dehydrogenase is encapsulated in a transparent porous silicate matrix by using sol-gel techniques. The inorganic polymer is formed around the enzyme (MW 〉 300,000 D). The enzyme is active in the material, catalyzes the reaction of L-glutamate to 2-oxoglutarate and follows Michaelis-Menten kinetics. The allosteric regulators ADP and GTP inhibit or activate the reaction; at pH 6, GTP acts as a strong activator and ADP acts as an inhibitor. This system involves a complex series of interactions; the co-enzyme NAD+ is required for catalysis, large-scale conformational changes accompany the binding of the substrate and coenzyme to the enzyme, the activators/inhibitors must bind to the enzyme to regulate the reactions, and the substrates and products must diffuse through the matrix to and from the binding site. The influence of the unique matrix on the complex enzymatic system is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008713014152
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  • 4
    Electronic Resource
    Electronic Resource
    Spectroscopic Determination of Cholinesterase Activity and Inhibition in Sol-Gel Media (1997)
    Springer
    Journal of sol gel science and technology 8 (1997), S. 1067-1070 
    Details
    ISSN: 1573-4846
    Keywords: cholinesterase ; sol-gel ; pesticide ; THA ; enzyme activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Biological activity of cholinesterases can be determined by optically monitoring the enzymatic reaction with indophenyl acetate, (N-4′-acetoxyphenyl)-4-quinone imine. At pH 8.0 cholinesterases hydrolyze this yellow dye to yield a blue reaction product. Cholinesterase inhibitors reduce the rate of this hydrolysis. Thus, by monitoring absorbance of the hydrolysis product at its maximum (630 nm) as a function of time, reaction rates of both cholinesterase activity and cholinesterase inhibition may be quantified spectroscopically. Using this technique, we measured the enzymatic activity of butyrylcholinesterase (BuChE) molecules encapsulated in tetramethyl orthosilicate (TMOS) silicate gel-glass prepared by hydrolysis and condensation. This activity is reduced, in a concentration-dependent manner, by the reversible cholinesterase inhibitors 1,5-bis(4-allyldimethyl-ammoniumphenyl) pentan- 3-one dibromide (BADAPP) and 9-amino-1,2,3,4-tetrahydroacridine (THA; tacrine, Cognex). The gel-glasses are rigid and compact, transparent, and porous enough to allow reagents to diffuse in and out.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018350828807
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    Paper (German National Licenses)
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