TABLE 1.
Purification of Atp8a2 from bovine rod outer segments by immunoaffinity chromatography
The activity of Atp8a2 was measured in the presence of 5 mm ATP and endogenous lipid concentrations following solubilization for the lysate and unbound fractions, respectively. For the elution fraction, 10% exogenous DOPS was added to maximally stimulate the ATPase activity.
| Fraction | Volume | Protein | Total PS-stimulated activity | Specific activity | Yield | Purification |
|---|---|---|---|---|---|---|
| μl | mg | nmol ATP/min | nmol ATP/min/mg | % | -fold | |
| Lysate | 490 | 1.59 | 0.232 | 28.67 | 100 | 1.0 |
| Unbound | 490 | 1.59 | 0.152 | 18.74 | ||
| Elution | 65 | 4.3 × 10−4 | 1.010 | 54,087 | 51 | 1,887 |