PubMed · 8330424
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P Nuutila, J Eskola. 1993. Incorrect FT4 assay buffer stated.. https://pubmed.ncbi.nlm.nih.gov/8330424/
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The chemical stability of nicotinamide adenine dinucleotide coenzyme (NADH/NAD+) and its derivatives (NADPH/NADP+) was investigated using changes in the UV-visible absorption spectra of these compounds. The spectra of cofactor (reduced form) were monitored at 340 nm wavelength in different buffers, showing a faster degradation in phosphate buffer. This was assigned to the adduct formation between phosphate and NADH (pyridine ring). The three-factor-two-level factorial design study evaluated the contributions: buffers (phosphate and Pipes 0.1 M), pH's (6.8 and 7.8), and temperature (25 and 30 degrees C). The freshly prepared aqueous solutions of coenzyme were analyzed after 40 min under the different conditions (eight assays in triplicate) of the experiment. The main observed effects of the NADH oxidation were, in increasing order, pH, temperature, and buffer without appreciable interactive effects. Therefore, it was verified that the better conditions for cofactor use were alkaline media employing Pipes buffer or its derivatives and low temperatures.
Capillary electrophoresis has been shown to be a very useful analysis technique for secondary metabolites of plants. In the present study a method is described for the qualitative and quantitative determination of ergot alkaloids and their epimers. The extraction from the biological matrix yields recoveries of 50-97%, depending on the individual alkaloid. Using a mixture of 20 mM beta-cyclodextrin (CD), 8 mM gamma-CD, 2 M urea and 0.3% (w/w) poly(vinyl alcohol) to phosphate buffer at pH 2.5 the simultaneous separation of all analytes was achieved. A 37 cm (30 cm) fused-silica capillary, at a voltage of 25 kV and a temperature of 20 degrees C, was used for the analysis. Overall analysis time for the separation was 12 min. The limit of detection of the alkaloids using UV detection at 214 nm can be improved 30-fold to about 9.10(-8) M when laser-induced fluorescence detection is applied.
The affinity of an antibody towards its antigen is highly specific to its conformation, in order to have optimal antibody-antigen interaction. The increase of temperature might cause changes in antibody conformations. The change of structure conformations may be reflected in the isoelectric points (pI values), peak shape and absorbance of the antibody. In this study, a monoclonal antibody was heated over a period of time. Capillary isoelectric focusing (cIEF) and capillary zone electrophoresis (CZE) were used to monitor the change in the antibody. The longer the heating period, the lower the pI values were under cIEF conditions. CZE also showed changes in peak shapes and decreases in absorbance of the antibody with heating.