抄録
Boundary electrophoretic behaviors of crystalline yeast PGA mutase have been studied in veronal and phosphate buffers. The crystalline enzyme used here is composed of five components.
Each component has been separated in a large quantity by using the special vertical zone electrophoresis apparatus with Hg-Hg2Cl2 reversible electrodes, which is deviced to compensate electroosmotic flow automatically.
The components I to IV are the PGA mutase protein and have different specific activities.
Each separated component has been crystallized by the dropwise addition of saturated ammonium sulfate solution.
The crystalline form of each component separated is the same as the original one.
