Table III.
Purification of LPA phosphatase from developing peanut cotyledons
| Fraction | Protein | Total Activity | Specific Activity | Purification |
|---|---|---|---|---|
| mg | nmol min−1 | nmol min−1 mg−1 | −fold | |
| Cytosol | 947 | 16 | 0.2 | 1 |
| Octyl-Sepharose | 17.2 | 97.2 | 5.7 | 33 |
| Blue Sepharose | 4.6 | 87.4 | 19.1 | 112 |
| Superdex 75 | 0.6 | 46.6 | 75.1 | 442 |
| Heparin-agarose | 0.03 | 25.7 | 858 | 5048 |
The results are the summary of a typical purification of the LPA phosphatase. Frozen immature seed (50 g) was used for preparing the soluble fraction. The enzyme activities were measured using 3H-LPA as a substrate. The purification steps are described under “Materials and Methods.”