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Freezing and vacuum-drying LDH in the presence of 300 mM trehalose resulted in the recovery of 80% and 65% of the original activity, respectively. For vacuum-dried mixtures, boron concentrations below 1.2 mole boron/ mole trehalose had no effect on recovered LDH. After several weeks storage in either humid ( relative humidity) or warm (45 ...
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The destabilizing effect of mannitol crystallization on LDH during freeze-drying can likely be attributed to removal of mannitol from the amorphous phase containing the protein. In addition, the formation of mannitol crystals seemed to enhance the interfacial denaturation of protein during freeze-drying. The use of 0.01% of Tween 80 in the ...
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The particle count was plotted as a function of aspect ratio to distinguish protein aggregates from air bubbles and dust particles. Thermally treated BSA and β-gal in sodium phosphate (100 mM) depicted a wide distribution of aspect ratio, a characteristic property of protein aggregates, owing to irregular morphologies (Fig. S2 in …
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HEC showed superior cryoprotective effects on LDH during freeze thawing, and considerable lyoprotective effects during the freeze drying process. Annealing had limited influence on the stabilizing effect of HEC. The extensive reconstitution times of the HEC lyophilisates could be greatly improved by incorporation of the surfactant Tween 80 into ...
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Fig. 3 shows the second-derivative IR spectra for LDH and LDH with the addition of Tween 80 at different temperatures. Each type of secondary structure gives a different C=O-stretching frequency in the spectrum. Strong bands near 1656 and 1636 cm −1 arise from α-helical and β-sheet structures, respectively (Prestrelski et al., 1993).The …
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3D profile of LDH concentration changes in the frozen bulk after regular (RF) and blast (BF) freezing. The initial LDH concentration was approximately 0.5 mg/mL in each bottle. The darker and larger the bubble, the more change in LDH concentration. Download : Download high-res image (761KB) Download : Download full-size image; Fig. 7.
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The objective of this study was to investigate the behavior of lactate dehydrogenase (LDH).upon freezing and thawing, alone or in the presence of several selected cryoprotectants. Also,-the influence of the freezing rate on retainment of LDH activity was investigated. It was observed that fast freezing caused less loss of LDH activity than slow …
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23280685. 10.1002/jps.23427. The objective of this study was to investigate the effect of histidine on the stability of the model protein lactate dehydrogenase (LDH) during freeze-drying. Several parameters were varied including pH of the bulk solution, histidine concentration, and performance of an annealing step during freezing.
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The objective of this study was to investigate the behavior of lactate dehydrogenase (LDH) upon freezing and thawing, alone or in the presence of several selected cryoprotectants. Also, the influence of the freezing rate on retainment of LDH activity was investigated. It was observed that fast freez …
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Lactate dehydrogenase is an enzyme that the body uses during the process of turning sugar into energy for your cells to use. LDH is found in many of the body's tissues and organs, including the muscles, liver, heart, pancreas, kidneys, brain and blood cells. The LDH test is mainly used to help identify the location and severity of tissue damage ...
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This test measures the level of lactate dehydrogenase (LDH), also known as lactic acid dehydrogenase, in your blood or sometimes in other body fluids. LDH is a type of protein, known as an enzyme. LDH plays an important role in making your body's energy. It is found in almost all the body's tissues, including those in the blood, heart, kidneys ...
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LDH showed improved stability in histidine buffer in comparison with other buffers. Protein stability and the tendency of histidine to crystallize during freeze‐drying were pH dependent. Annealing destabilized LDH and resulted in a decrease of the activity recovery. However, the extent of protein destabilization caused by annealing appears to ...
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LDH, at a high concentration (1000 µg/mL), has a pronounced self-stabilizing effect and did not aggregate after 5 freeze-thaw cycles. At lower LDH concentrations (10 and 100 µg/mL), irreversible aggregation could be avoided only with the selection of an appropriate buffer. While SANS provided evidence of the existence of aggregation, DLS ...
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An instability equation (%PD=−0.14*time (h)) adjusted using the least squares method was designed. Pearson's correlation coefficient (R) was 0.87 and a gradient far from 0 was obtained. This equation shows a daily loss of stability of 3.4%. In other words, for a MAD of 6.39%, the limit of stability was 45 h ( Figure 1 ).
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Individual formulation containing LDH (0.5 mL) was filled into 2-mL vials, and the vials were subsequently semistoppered.Freeze-drying experiments were performed using a FTS Lyostar TM II (SP Scientific, Gardiner, New York). Samples were loaded onto the shelves at room temperature, frozen using a 1° C/min shelf cooling rate down …
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Pharmaceutical Research. 2004. TLDR. The endothermic transformation of a PEG-ice structure at −15°C in the heating process is strongly correlated to the protective ability of PEG 6000 in the freeze-thawing process of LDH, where two phases of different crystallinity and stability might be involved. 12.
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