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

Joseph W. Turek and Guy C. Le Breton, Department of Pharmacology, University of Illinois at Chicago, College of Medicine, Chicago, IL 60612. Address correspondence to: Joseph W. Turek, 835 South Wolcott, Department of Pharmacology M/C 868, University of Illinois at Chicago, Chicago, IL 60612. E-mail: jturek1@icarus.uic.edu


Introduction

The human platelet thromboxane A2 (TXA2) receptor, in addition to its normal role in hemostasis, has been implicated in the pathogenesis of multiple cardiovascular diseases.1 Studies suggests that increased platelet production of the natural ligand, TXA2, may lead to enhanced platelet aggregatory activity, predisposing an individual to spontaneous platelet aggregation, followed by thrombus formation. Attempts to develop specific antagonists to block the TXA2 receptor have been hampered by a lack of information concerning the receptor ligand-binding domain.

Labeling of receptors, followed by sequential receptor digestion, accumulation, and sequence identification of labeled fragments, has become a commonly used approach to identify receptor ligand-binding domains.26 However, the initial digestion product contains a wide mixture of proteins, from smaller peptides which cannot be separated by traditional glycine gel electrophoresis, to larger proteins not effectively purified using reversed-phase or size exclusion HPLC. In addition, the limited availability of certain receptor proteins (including the TXA2 receptor) has hindered the isolation of sufficient amounts of labeled fragments. To circumvent these problems, we have coupled continuous elution preparative gel electro
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