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The latter preparations have the advantage of exhibiting minimal change in Q−A with either time or illumination at 1.7 K.
The latter preparations also revealed unique tubular-like particles.
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The latter preparation method showed superhydrophobic properties with static contact angles reaching up to 164° and contact angle hysteresis reaching as low as 2.5°.
For the latter preparation, the freeze-dried residues of the initial starting material (0 h) and at the end of the fermentation (96 h) was treated with a two-step H2SO4 hydrolysis following NREL/TP-510-42618 (Sluitet et al. 2008).
Nevertheless, this latter preparation method also requires a high temperature treatment step to form highly active catalysts in furfural/acetone aldol condensation because the ethoxy residues originated during aerogel preparation need to be removed.
Owing to the latter preparation having a high protein content, the enzyme precipitated on thawing.
The latter preparation of enzyme exhibited higher activity and was thus utilized unless otherwise specified.
The latter preparation had a higher protein concentration, resulting in many films with too many overlapping particles.
These contractile impairments were caused by stable modification(s) since they were observed even after isolation of myofibrils and single-muscle fibres, and the contractile impairments in the latter preparation were not affected by subsequent exposures to an oxidising (t-BuOOH) or a reducing (DTT) agent.
The IC50 values of VAP-Qu, VAP-M and VAP-A for the various breast and bladder carcinoma cell lines were lower than those obtained with VAP-P, indicating that this latter preparation has the weakest effect on viability/proliferation of carcinoma cells among the four VAPs tested.
For the latter, membrane preparations were obtained from capsule-plus-epithelial specimens, and from three cortical fractions, i.e. the anterior, equatorial, and posterior regions, as well as a fifth, nuclear fraction.
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