If the water of hydration of a protein dissolved in water is reduced by the addition of a salt such as ammonium sulfate, the protein is no longer soluble and is salted out, or precipitated.
Preanalytic testing: MIRIS was capable to measure bovine protein dissolved in water accurately.
Ninety-six well polystyrene microtiter plates were coated with various concentrations of protein, dissolved in 0.1 mol/L Na bicarbonate (pH 9.0).
The oxidized form was obtained from the purified protein dissolved in water at approximately 1 mg/mL and then exposed to air for approximately a week at room temperature and pH 7.2.
Solubilized Aβ40 (5 µM) was mixed with a protein dissolved in a respective buffer.
5 10 µL of protein, dissolved at 10 20 mg/mL, was incubated with a range of proteases for thirty minutes at room temperature.
The purified protein, dissolved in 6M urea, was dialyzed against phosphate buffered saline (PBS) to obtain a physiological preparation that was stored at −20°C.
As for the HSA irradiated with 30 kGy, a low increase of absorbance was noticed between 300 and 460 nm with the protein dissolved in either water or HEPES buffer (Fig. 2E).
Preparative 2D-PAGE was performed on 1 mg total cellular protein dissolved in sample buffer.
Media alone and soluble, freshly filtered protein dissolved in media were injected to serve as baseline for our experiments.
