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The best micrographs, obtained with the TorsinA(E171Q):LULL1 preparation, were further processed.
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For Au/TiO2, the effect of catalyst preparation was further investigated.
For amino acid sequence determination, the Natto peptide preparation was further purified by column chromatography on Wakosil-5C18HG column (Wako Pure Chemical, Tokyo, Japan).
The LPS preparation was further de-proteinated by TCA precipitation (5%), followed by dialysis and lyophilisation.
This MAR preparation was further checked for the enrichment of known MARs [ 22, 29].
The quality of the enzyme preparation was further assessed using a 2100 Bioanalyzer (Agilent Technologies).
This raw preparation was further purified by Nycodenz gradient centrifugation and the virion band harvested (Döhner et al., 2006).
To eliminate non-supercoiled plasmid forms, the plasmid preparation was further purified using CsCl-gradient ultracentrifugation [ 75].
The Tox preparation was further purified by passing it through a Sephadex G100 column and the active fractions were collected and lyophilised.
If the final protein concentration was below 1 mg/ml, the preparation was further concentrated using Vivaspin-6 or -20 (5000 MW PES, Sartorius AG, Göttingen, Germany).
This preparation was further disaggregated by pipetting and tissue debris and cardiomyocytes were removed by sequential centrifugation at 100 g for 2 minutes, passage through 20 μm sieve, and centrifugation at 400 g for 5 minutes.
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