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  • 1
    Electronic Resource
    Electronic Resource
    Microdetermination of mercury by the oxygen bomb combustion method (1968)
    s.l. : American Chemical Society
    Analytical chemistry 40 (1968), S. 2042-2043 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac60269a049
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  • 2
    Electronic Resource
    Electronic Resource
    Determination of Cardenolides in Hairy Root Cultures of Digitalis lanata by Enzyme-Linked Immunosorbent Assay (1990)
    s.l. : American Chemical Society
    Journal of natural products 53 (1990), S. 1498-1502 
    Details
    ISSN: 1520-6025
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/np50072a015
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  • 3
    Electronic Resource
    Electronic Resource
    Production and characterization of a specific monoclonal antibody against mycotoxin zearalenone (1990)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 38 (1990), S. 1618-1622 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf00097a040
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  • 4
    Electronic Resource
    Electronic Resource
    Stability of β-Galactosidase, a Model Protein Drug, Is Related to Water Mobility as Measured by 17O Nuclear Magnetic Resonance (NMR) (1993)
    Springer
    Pharmaceutical research 10 (1993), S. 103-108 
    Details
    ISSN: 1573-904X
    Keywords: β-galactosidase ; protein stability ; water mobility ; lyophilization ; 17O nuclear magnetic resonance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The inactivation of freeze-dried β-galactosidase during storage was studied, focusing on the effect of water mobility as measured by the spin-lattice relaxation time, T 1, of water using 17O NMR. Inactivation of β-galactosidase lyophilized from phosphate buffer solution was studied as a function of water content, which in turn affected the T l of water. An increase in the water content of freeze-dried β-galactosidase brought about an increase in the T l of water, as well as a rise in pH. For the freeze-dried enzyme with sufficient water content to be dissolved, the inactivation rate was related to the T l of water rather than to the pH change. It is suggested that as the water content increases, the mobility of water around the enzyme increases, resulting in enhanced enzyme inactivation. The freeze-dried samples with limited moisture showed inactivation rates faster than those expected from the pH and water mobility, suggesting that the inactivation mechanism is different from that for the freeze-dried enzyme with a larger amount of water. Inactivation of β-galactosidase in solutions was also studied as a function of phosphate buffer and sodium chloride concentrations, which in turn affected the T l of water. Because the inactivation rate increased with increasing salt concentrations and the rate extrapolated to zero concentration was negligible, inactivation of the freeze-dried enzyme was apparently induced by the salts used as additives for lyophilization. The enhancing effect of phosphate buffer components, however, was reduced at higher concentrations, an effect related to the decrease in the T l of water. This result may be ascribed to the decrease in water mobility caused by phosphate buffer components and is consistent with the observation that the inactivation rate of the freeze-dried enzyme with a relatively large amount of water decreased with decreasing T 1 of water.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018933315538
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  • 5
    Electronic Resource
    Electronic Resource
    The Effect of Salts on the Stability of β-Galactosidase in Aqueous Solution, as Related to the Water Mobility (1993)
    Springer
    Pharmaceutical research 10 (1993), S. 1484-1487 
    Details
    ISSN: 1573-904X
    Keywords: β-galactosidase ; stability in solution ; water mobility ; spin lattice relaxation time
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The effect of salts (KI, KBr, NaCl, KC1, KF, phosphate, and Na2SO4) on the stability of β-galactosidase in aqueous solution was studied from the aspect of changes in water mobility. At salt concentrations up to 200 mM, the inactivation rate of β-galactosidase in all the salt solutions studied increased with increasing salt concentration. At higher concentrations, those salts which had little effect on the spin-lattice relaxation time, T 1, of water (KI, KBr, and KC1) continued to increase the inactivation rate of β-galactosidase with increasing concentration, while those salts which decreased the T l of water (KF, phosphate, and Na2SO4) decreased the inactivation rate. It appeared that the decrease in water mobility caused by KF, phosphate, and Na2SO4 resulted in stabilization of β-galactosidase. The results indicate that water mobility is an important factor in the denaturation rate of proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018931527176
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  • 6
    Electronic Resource
    Electronic Resource
    Aggregates Formed During Storage of β-Galactosidase in Solution and in the Freeze-Dried State (1993)
    Springer
    Pharmaceutical research 10 (1993), S. 687-691 
    Details
    ISSN: 1573-904X
    Keywords: β-galactosidase ; aggregation ; solution ; freeze-dried
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Aggregates formed during storage of freeze-dried β-galactosidase were compared with those formed in solutions. Freeze-dried β-galactosidase aggregated during storage in the presence of moisture, producing a protein precipitate which was soluble in guanidine hydrochloride solution but not in buffer solution. The protein precipitate dissolved in guanidine solution exhibited a large molecular size by high-performance size exclusion chromatography and converted to proteins of original size in the presence of dithiothreitol. It is suggested that the aggregation involves chemical interaction via covalent disulfide bonding. In contrast, β-galactosidase in aqueous solution aggregated without formation of protein precipitates. Soluble aggregates were converted to proteins of original size in guanidine solution without dithiothreitol, suggesting noncovalent bonding. The difference in aggregation behavior may be ascribed to the difference in the water:protein ratio. We propose that inactivation of β-galactosidase is due to formation of thermally denatured (unfolded) protein, which aggregates dependent on the water:protein ratio, either via noncovalent interactions at a high water:protein ratio in solution or via covalent interaction at a low water:protein ratio in the freeze-dried state.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018951530927
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  • 7
    Electronic Resource
    Electronic Resource
    Decreased Protein-Stabilizing Effects of Cryoprotectants Due to Crystallization (1993)
    Springer
    Pharmaceutical research 10 (1993), S. 1232-1237 
    Details
    ISSN: 1573-904X
    Keywords: freeze-drying ; protein-stabilizing effects ; cryoprotectants ; crystallization ; β-galactosidase ; mannitol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The stabilizing effects of various additives against inactivation of an enzyme (β-galactosidase from Aspergillus oryzae) during freeze-drying were studied, with a focus on their crystallinity. The crystalline morphology of mannitol and inositol in freeze-dried cakes depended on the solute concentrations before freezing and the freeze-drying method used. The additives in their amorphous state showed concentration-dependent stabilization of the enzyme, whereas additive crystallization during freeze-drying decreased their effects. Heat treatment before freeze-drying also caused crystallization and diminished the stabilizing effects. Noncovalent soluble aggregates were observed in the inactivated enzyme solution. These results show the importance of maintaining the amorphous state of additives used as stabilizing agents during freeze-drying.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018988823116
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  • 8
    Electronic Resource
    Electronic Resource
    Estimation of Agitation Intensity in the GI Tract in Humans and Dogs Based on in Vitro/in Vivo Correlation (1995)
    Springer
    Pharmaceutical research 12 (1995), S. 237-243 
    Details
    ISSN: 1573-904X
    Keywords: absorption ; dissolution tests ; hydrodynamic flow in GI tract ; controlled release ; in vitro/in vivo relationship ; acetaminophen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract In this study, we assessed the hydrodynamic flow around a dosage form in the GI tract in humans by comparing the characteristics of in vitro and in vivo release of two different types of controlled release acetaminophen (paracetamol) tablets, A and B. The former tablet showed an agitation speed-dependent release at a high speed range (50–100 rpm), whereas the latter showed this characteristic at a low speed range (10–50 rpm). The mean release amount-time profiles of tablets A and B in humans showed biphasic characteristics, and the first phase of the absorption profiles of A and B was close to their in vitro profiles at a paddle speed of 10 rpm. The in vivo profiles were also superimposable on in vitro dissolution curves obtained by the flow-through cell method at a flow rate of 1 mL/min (velocity 0.89 cm/min) or less. These results indicate that the hydrodynamic flow around the dosage forms in the human GI tract could be extremely low. The in vivo release rate of these tablets in dogs was greater than in humans, and was estimated to be equivalent to the release rate determined by the paddle method at 100 rpm. This indicates that a higher agitation intensity in the GI tract in dogs than in humans may be one cause of the discrepancies between humans and dogs in drug absorption studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1016231010301
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  • 9
    Electronic Resource
    Electronic Resource
    Effect of Water Mobility on Drug Hydrolysis Rates in Gelatin Gels (1992)
    Springer
    Pharmaceutical research 9 (1992), S. 607-612 
    Details
    ISSN: 1573-904X
    Keywords: gelatin ; gel ; hydrolysis ; mobility ; nuclear magnetic resonance (NMR) ; electron spin resonance (ESR) ; dielectric relaxation spectroscopy ; trichlormethiazide ; flomoxef
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The stability of drugs incorporated in gelatin gels was studied, with a focus on the water mobility in the gels. Trichlormethiazide hydrolysis and kanamycin-catalyzed flomoxef hydrolysis in gelatin gels were chosen as models for apparent first-order and second-order hydrolysis, respectively. The mobility of water in gelatin gels was determined by NMR, ESR, and dielectric relaxation spectroscopies. The amount of bound water in the gels was determined from dielectric relaxation spectra. Spin-lattice relaxation time of water determined by 17O NMR and rotational correlation time of an ESR probe determined by an ESR probing method were useful in determining the micro viscosity of the gels. The hydrolysis rate of trichlormethi-azide in the gels was found to depend on the amount of free water available for the reaction, while that of flomoxef depended on the micro viscosity of the gels, which reflected the mobility of water molecules. Thus the dependence of hydrolysis rates on the water mobility was influenced by the hydrolysis mechanism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015837723851
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  • 10
    Electronic Resource
    Electronic Resource
    Entrapment of Proteins in Poly(L-Lactide) Microspheres Using Reversed Micelle Solvent Evaporation (1994)
    Springer
    Pharmaceutical research 11 (1994), S. 337-340 
    Details
    ISSN: 1573-904X
    Keywords: protein ; poly(L-lactide) ; microspheres ; reversed micelles
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018936314861
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