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

base, pH to 8.9 with HCl) in the lower and elution chambers. The apparatus was operated at 4 watts constant power until the dye front migrated to the bottom of the tube gel. At this time, the tube gel was connected to a peristaltic pump (flowing at a rate of 0.1 ml/min), and 1 ml fractions were isolated for the next 16 hours. Fractions were concentrated by lyophilization and subsequently resuspended in a small volume of buffer (250 l).


Results

Tricine SDS-PAGE slab gels (16.5%) were stained by Coomassie brilliant blue and used to identify fractions containing CNBr digested TXA2 receptor protein in the eluate from the Mini Prep Cell. These gels have been described by Schagger and von Jagow to optimally separate low molecular weight proteins.7 As shown in Figure 1, this procedure resulted in the separation of low molecular weight CNBr digested TXA2 receptor fragments (3.517 kD) into discrete bands. Under these conditions, proteins with a molecular weight difference as low as 23 kD could be effectively resolved. The bands corresponding to labeled fragments can then be sequenced to reveal their amino acid composition.


Conclusions

The procedure outlined in this bulletin offers a highly effective method for separating low molecular weight proteins using the Mini Prep Cell. In this system, the substitution of tricine for glycine in the running buffer and the use of a low pH gel buffer prevents the low molecular proteins from spreading as they unstack within the gel, resulting in sharper bands as low as 3.5 kD. Additionally, since the proteins are obtained in solution, traditional electro-eluti
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