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  • 1
    Electronic Resource
    Electronic Resource
    The singular values of involutory and of idempotent matrices (1963)
    Springer
    Numerische Mathematik 5 (1963), S. 234-237 
    Details
    ISSN: 0945-3245
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01385894
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  • 2
    Electronic Resource
    Electronic Resource
    Apparent retrograde metamorphism: Another example of the influence of structural deformation on metamorphic differentiation (1968)
    Springer
    Contributions to mineralogy and petrology 17 (1968), S. 173-186 
    Details
    ISSN: 1432-0967
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences
    Notes: Abstract A model relating apparent retrograde metamorphism to folding is proposed. According to the model, pressure gradients brought on by folding in the course of regional metamorphism cause the migration of water to low pressure fold crests. The greater concentration of water renders the mineral assemblage unstable relative to a more hydrous, “lower grade” assemblage. The result is that several mineral assemblages, each of which is characteristic of what classically has been called a different metamorphic facies, can be formed during the same metamorphic event, under the same pressure-temperature conditions. As an example, the paragenetic relationships between three mineral assemblages in a metamorphosed basalt flow are explained in terms of chemical changes accompanying structural deformation. During regional metamorphism the basalt was recrystallized to hornblende-, oligoclase-, and biotite-bearing assemblages. Folding late in the course of the regional metamorphism brought about the destruction of pre-existing assemblages in the fold crests and formation there of a more hydrous chlorite and albite assemblage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00388942
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  • 3
    Electronic Resource
    Electronic Resource
    Phase II evaluation of teniposide (VM-26) in metastatic breast carcinoma (1988)
    Springer
    Investigational new drugs 6 (1988), S. 37-40 
    Details
    ISSN: 1573-0646
    Keywords: breast cancer ; breast carcinoma ; teniposide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Abstract The Southeastern Cancer Study Group performed a Phase II study of teniposide in previously treated patients with metastatic breast cancer. No responses were observed in 11 evaluable patients who received teniposide 60 mg/m2 by IV infusion for five consecutive days every three weeks. Toxicity was primarily gastrointestinal and hematologic and was frequently severe. This study demonstrated no therapeutic activity for teniposide when given in this dose and schedule to patients with heavily pretreated metastatic breast cancer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00170777
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  • 4
    Electronic Resource
    Electronic Resource
    Development of a Stable Freeze-dried Formulation of Recombinant Human Interleukin-1 Receptor Antagonist (1996)
    Springer
    Pharmaceutical research 13 (1996), S. 243-249 
    Details
    ISSN: 1573-904X
    Keywords: freeze-dried formulation ; rhIL-lra ; protein stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. A formulation of recombinant human interleukin-1 receptor antagonist (rhIL-1ra) was developed that provided both acute protection during lyophilization and storage stability in the dried solid. Methods. The formulation was optimized by monitoring the impact of excipients on protein degradation which was analyzed by turbidimetry and cation-exchange HPLC. Results. The most appropriate pH was 6.5. Sodium citrate buffer provided better stability than sodium phosphate buffer. Glycine was selected as a bulking agent because the greatest protein stability was noted when this bulking agent was used in combination with an amorphous protein stabilizer. Among the amorphous stabilizers tested, sucrose protected rhIL-lra best in the presence of glycine. When the protein was freeze-dried in the presence of an inadequate mass ratio of sucrose/protein (〈 0.3), the rate of degradation of rhIL-lra increased. For a formulation containing 100 mg/ml of rhIL-lra, increasing the sucrose/protein mass ratio to ≥ 0.3 greatly increased storage stability. The moisture content of the dried solid affected the storage stability to a minor degree. Three different stoppers obtained from the WEST Company did not affect the stability of rhIL-lra. Conclusions. An optimized formulation could be reconstituted without precipitation after 14 months at 30 or 50°C. At 30°C, there was no loss of native protein due to deamidation, and only a 4% loss at 50°C. These results indicated that the optimized formulation could be stored at ambient temperatures for long periods, without damage to the protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1016043114998
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  • 5
    Electronic Resource
    Electronic Resource
    Effects of Sugars and Polymers on Crystallization of Poly(ethylene glycol) in Frozen Solutions: Phase Separation Between Incompatible Polymers (1996)
    Springer
    Pharmaceutical research 13 (1996), S. 1393-1400 
    Details
    ISSN: 1573-904X
    Keywords: frozen solution ; phase separation ; poly(ethylene glycol) ; crystallization ; molecular interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. This study examined the effect of third components (low-molecular-weight saccharides and polymers) on the crystallization of poly(ethylene) glycol (PEG) in frozen solutions, focusing on the relationship between their crystallization-inhibiting ability and molecular compatibility. Methods. Effects of sugars and polymers on the crystallization of PEG 3000 in frozen solution were monitored by differential scanning calorimetry (DSC). Pulsed-NMR was employed to monitor the molecular mobility of water and solutes in the frozen solutions. Miscibility between PEG and third components in aqueous solution was estimated from the lowering of cloud point of PEG 20,000. Thermal analysis of frozen solutions containing some non-crystallizing solutes was used to examine the possibility of phase separation in frozen solutions. Results. Some sugars and polymers inhibited the crystallization of PEG and formed practically stable amorphous phases among ice crystals. The mobility of solute molecules in the amorphous phase increased above the softening temperature of maximally concentrated solutions (Ts), whereas that of water molecules appeared at a lower temperature. Mono- and disaccharides that are relatively less miscible with PEG in solution inhibit PEG crystallization to a lesser degree. Two Ts regions were observed in frozen solutions containing both polyvinylpyrrolidone (PVP) and dextran, at much lower concentrations than those causing aqueous two-phase separation at ambient temperatures. Conclusions. Ice crystallization raises the concentration of solutes in the remaining solution, which can lead to phase separation in the amorphous phase. Molecular compatibility between components is an important factor determining their propensity to phase separate and crystallize.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1016086319851
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  • 6
    Electronic Resource
    Electronic Resource
    Real-Time in Situ Monitoring of Lysozyme During Lyophilization Using Infrared Spectroscopy: Dehydration Stress in the Presence of Sucrose (1997)
    Springer
    Pharmaceutical research 14 (1997), S. 1548-1555 
    Details
    ISSN: 1573-904X
    Keywords: FTIR spectroscopy ; attenuated total reflectance ; internal reflection ; lyophilization ; lysozyme ; sucrose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. First, to investigate the role of sucrose in stabilizing protein structure (as measured by changes in the amide I band of lysozyme) caused by dehydration encountered during lyophilization. Second, to demonstrate the utility of internal reflection spectroscopy as a tool for conducting controlled lyophilization experiments. Methods. A custom-built internal reflection FTIR accessory was used to follow the entire freeze-drying process of solutions consisting of 49.4 mg/mL lysozyme in the presence and absence of 10% sucrose in real-time. Studies were carried out using D2O as a transparent medium in the infrared region of the protein amide bands. Potential self-association of the protein in the presence of sucrose was investigated using dynamic light scattering. Hydration levels were determined using a multiple regression equation. Differential scanning calorimetry (DSC) permitted characterization of the final lyophilized product. Moisture content was determined using Karl Fischer titration. Results. Throughout freezing and drying, minimal changes were observed both in frequency (1647 ± 1 cm−1) and bandwidth (46 ± 1 cm−l) of the amide I band in the presence of sucrose. In contrast, greater changes in frequency and band width were seen in the absence of sucrose. A successfully lyophilized cake was obtained which had properties of a glass as measured by DSC, with a Tg of 50°C. The lyophilized product containing sucrose had 4% moisture by weight. Three distinct rates of water desorption were discovered during drying under vacuum (50 mg/hr within the sample temperature range from −35° to −25°C; 30 mg/hr from 10° to 25°C; 1.2 mg/hr from 27° to 38°C). Conclusions. The inclusion of sucrose served to minimize perturbations of protein structure caused by freezing and dehydration stresses encountered during lyophilization (compared to studies conducted in the absence of sucrose). The results support the water replacement hypothesis and underscore the role of the sugar in preserving a native structure in the dried state. This investigation demonstrates the usefulness of infrared spectroscopy in evaluating lyophilization process parameters and formulation design.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1012170116311
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  • 7
    Electronic Resource
    Electronic Resource
    Thermal Stability of Low Molecular Weight Urokinase During Heat Treatment. II. Effect of Polymeric Additives (1994)
    Springer
    Pharmaceutical research 11 (1994), S. 1004-1008 
    Details
    ISSN: 1573-904X
    Keywords: protein stability ; aggregation ; turbidimetry ; urokinase ; formulation ; additives, polymeric
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Turbidimetric or light scattering assays can be used to determine the extent of aggregation in protein formulations. Using low molecular weight urokinase (LMW-UK) as a model protein, the effect of polymeric additives on heat-induced aggregation was evaluated. Previous work has shown that under 60°C heat treatment, LMW-UK initially denatures and the unfolded protein associates to form soluble aggregates. Eventually, these aggregates associate to form a precipitate. The effects of polymers on the initial aggregation phase was examined. Hydroxyethyl (heta) starch, polyethylene glycol 4000, and gelatin were found to be effective, concentration-dependent inhibitors of aggregation, whereas polyvinylpyrrolidone (PVP) and polyethylene glycol 300 were ineffective. Overall, the effect of polymeric additives on the stability of thermally-stressed LMW-UK can be accounted for by preferential exclusion of the solute from the surface of the protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018935420680
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  • 8
    Electronic Resource
    Electronic Resource
    Rational Design of Stable Lyophilized Protein Formulations: Some Practical Advice (1997)
    Springer
    Pharmaceutical research 14 (1997), S. 969-975 
    Details
    ISSN: 1573-904X
    Keywords: protein drugs ; design of formulations ; lyophilization ; stabilization of proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1012180707283
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  • 9
    Electronic Resource
    Electronic Resource
    Arrestment of carbohydrate metabolism during anaerobic dormancy and aerobic acidosis inArtemia embryos: determination of pH-sensitive control points (1986)
    Springer
    Journal of comparative physiology 156 (1986), S. 451-459 
    Details
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Changes in concentrations of trehalose, glycogen, glycerol, some glycolytic intermediates and adenylate nucleotides that occur during aerobic development have been compared to those seen during anaerobic dormancy and aerobic acidosis in gastrula-stage embryos ofArtemia. The latter two incubation conditions are known to foster large drops in intracellular pH (Busa et al. 1982; Busa and Crowe 1983). During aerobic development, trehalose levels decline while glycogen and glycerol are synthesized (Fig. 1). These transitions are blocked during both anaerobic dormancy and aerobic acidosis, but are resumed by return of embryos to aerobic incubation (Fig. 1). Thus, it is concluded that carbohydrate catabolism in hydrated embryos is directly modulated by intracellular pH. Changes in metabolite levels (Figs. 2–4) reveal that this process is controlled primarily at the trehalase and hexokinase reactions with a less-pronounced negative crossover point noted at the phosphofructokinase step. Each of these reactions is shown to be nonequilibrium by comparing the mass action ratio to the equilibrium constant (Table 1). When embryos are placed under anaerobic conditions, ATP levels drop dramatically while AMP increases in concentration (Fig. 5). These changes are reflected in a drop in adenylate energy charge from a control value of 0.73 to 0.42 (Fig. 6). Aerobic acidosis only leads to a slight decrease in energy charge, emphasizing that shifts in adenylate pools
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00691030
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  • 10
    Electronic Resource
    Electronic Resource
    Stability of Human Serum Albumin During Bioprocessing: Denaturation and Aggregation During Processing of Albumin Paste (2000)
    Springer
    Pharmaceutical research 17 (2000), S. 391-396 
    Details
    ISSN: 1573-904X
    Keywords: albumin ; human serum ; aggregation ; bioprocessing ; plasma proteins ; infrared spectroscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. To assess the impact of various bioprocessing steps on thestability of freshly precipitated human serum albumin (HSA) obtainedfrom pooled human plasma.Methods. After initial precipitation of HSA from plasma, the resultantpaste is either (a) lyophilized or (b) washed with acetone and thenair-dried in order to obtain a dry powder. The structure of HSA wasexamined using Fourier transform infrared (IR) spectroscopy. Theextent of aggregation of redissolved HSA was measured using bothdynamic light scattering and SDS-polyacrylamide gel electrophoresis(SDS-PAGE).Results. Both lyophilization and air-drying perturb the secondarystructural composition of HSA, as detected by infrared (IR) spectroscopy.Upon dissolution of dried paste, most of the protein refolds to anative-like conformation. However, a small fraction of the protein moleculesform soluble aggregates that can be detected by both dynamic lightscattering and SDS-PAGE. The level of aggregation is so low that itcould not be detected in the bulk by either circular dichroism orIR spectroscopy. The lyophilized protein, which appears to be moreunfolded in the solid state than the acetone washed/air-dried material,exhibits a higher level of aggregation upon dissolution.Conclusions. There is a direct correlation between the extent ofunfolding in the solid state and the amount of soluble aggregate presentafter dissolution. Moreover, the presence of the aggregates persiststhroughout the remainder of the purification process, which includesdissolution, chromatography, sterile filtration and viral inactivationsteps. Analytical methods used to monitor the stability ofbiopharmaceuticals in the final product can be used to assess damage inflictedduring processing of protein pharmaceuticals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007564601210
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