1. Reported effects of different conditions on the stability of the purified chlorophyll-protein complex have been confirmed.
2. The electrophoretic behavior of the chlorophyll-protein complex prepared from two unrelated species of plants (Aspidistra elatior and Phaseolus vulgaris) has been investigated and shown to be dissimilar. In M/50 acetate buffer at 25°C, the isoelectric point of the complex from Phaseolus is at pH 4.70, whereas that from Aspidistra is at pH 3.9 (extrapolated). These values fall within the usual range of protein isoelectric points.
3. Treatment with weak acids causes an irreversible denaturation of the protein complex from both species, with a resultant shift in the mobility-pH curves to more basic values.
4. Differences in electrophoretic behavior between the chlorophyll-protein complex and the cytoplasmic proteins of Phaseolus have been demonstrated. The isoelectric point of the latter is at pH 4.22.
