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Isolation of Low Molecular Weight Digestion Products of the Human Platelet Thromboxane A2 Receptor, Rev A

resulting in a final protein concentration of 1 mg/ml. Cyanogen bromide (CNBr) crystals were then added in 100 times molar excess over methionine residues in the protein, with digestion carried out at room temperature, while tilting the solution for 2436 hours in the dark. Digestion was terminated by diluting the sample solution to 7% formic acid with deionized water, immediately followed by lyophilization. Digested protein was then resuspended in 600 l deionized water and added to 150 l of 5x sample buffer (125 mM Tris-base, 30% glycerol, 10% SDS, 5% -mercaptoethanol, and 0.25% Coomassie blue G-250, pH to 6.8 with HCl). Samples were denatured at 50 C for 45 minutes prior to loading onto the preparative electrophoresis gel.

TRICINE CONTINUOUS ELUTION ELECTROPHORESIS
The Mini Prep Cell was assembled with a single modification to the manufacturers instructions. A dialysis membrane of 100 Dalton molecular weight exclusion limit was used to replace the 3.5 or 6 kD membrane supplied by the manufacturer. This modification prevents desirable low molecular weight proteins from passing through the dialysis membrane. Table 1 shows the gel composition for the 16.5% tricine gels used in these experiments. The separating gel was poured to a height of 6.67 cm and immediately followed by a 1.33 cm spacer gel. After these layers had polymerized sufficiently, a 2 cm stacking gel was cast over the spacer gel. Following complete polymerization, the gels were stored at 4 C overnight to allow equilibration. The next day, electrophoresis was carried out in the coldroom (4 C) using tricine cathode buffer (100 mM Trisbase, 100 mM tricine, 0.1% SDS, pH 8.25) in the upper chamber, and anode buffer (200 mM Tris-
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