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The lipid shell of the hybrid NP was quickly disintegrated in buffer with a pH of 5.5, which resembles the acidic environment of endosomes in dendritic cell (DC).
When incubated (40°C) in buffer with a pH between 5.4 and 6.0, 7B had about 10 to 25 times greater amylase activity than AMA, and enzyme activity in this range increased by 100% for 7B, whereas activity decreased by about 26% for AMA.
Buffer solutions of 2- N-morpholino)ethanesulfonic acid buffer with a pH of 6.1 and Tris buffer with a pH of 7.8 were prepared freshly before each use.
Separated RCs were suspended in a 0.01-M Na-P buffer with a pH of 7.2, which contained 0.05 % LDAO [18].
The reaction mixture contained 56 μM NBT, 0.01 M methionine, 1.17 μM riboflavin, 20 μM NaCN and 0.05 M phosphate buffer with a pH of 7.8.
The conjugation of anti-CAIX with SCN-Bz-DTPA or SCN-Bz-DOTA (Macrocyclics, Dallas, TX, USA) with a 50-fold molar excess was performed in a 0.1 M NaHCO3 buffer, with a pH of 8.2.
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In the experiment for estimation of optimum pH, McIlvaine buffers with a pH range 3.0-8.0 3.0-8.0ed.
The methylation reaction was carried out in presence of 50 nM HP0593 MTase, 2.5 µM of duplex 2, 1.5 µM [methyl-3H] AdoMet, and in buffers with a pH range of 3.5 to 8.5.
McIlvaine buffers with a pH range from 3.0 to 8.0 were used.
Yeast cells were exposed to advanced starvation conditions using buffers with a pH of 6, 7 or 8 for 3 days.
For pH-stability assay, the enzyme was preincubated in buffers with a pH range of 4.0 10.0 for 1 h at 37°C, and then the residual activities were examined under standard conditions (pH 6.0, 40°C, and 10 min).
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