THE ACTION OF SODIUM DODECYL SULFATE ON THE CHLOROPHYLL-PROTEIN COMPOUND OF THE SPINACH LEAF.
1. Sodium dodecyl sulfate (SDS) attacks the chlorophyll-protein compound modifying its protein properties and absorption spectrum. 2. In the presence of SDS, chlorophyll is quantitatively converted to phaeophytin; i.e., magnesium is removed from the molecule. This reaction, measured spectrophotometrically, proceeds at a rate directly proportional to the hydrogen ion concentration. At constant pH, the rate is proportional to the SDS concentration until a maximum rate is achieved. 3. The chlorophyll or phaeophytin (depending on the pH) remains attached to the protein, since the prosthetic group cannot be separated by ultrafiltration, dialysis, or fractional precipitation. 4. This suggests that the magnesium plays no part in binding chlorophyll to the split protein fragments, but may be concerned in binding the larger units, since the metal becomes extremely labile when the protein is split.
Smith
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Laboratory of Biophysics, Columbia University, New York, and the Molteno Institute, University of Cambridge, England.