Isolation of the fibrinogen-binding region of platelet thrombospondin |
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Authors: | V M Dixit G A Grant W A Frazier S A Santoro |
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Affiliation: | 1. Division of Laboratory Medicine Washington University School of Medicine St. Louis, Missouri 63110 USA;2. the Department of Pathology Washington University School of Medicine St. Louis, Missouri 63110 USA;3. the Department of Medicine Washington University School of Medicine St. Louis, Missouri 63110 USA;4. the Department of Biological Chemistry Washington University School of Medicine St. Louis, Missouri 63110 USA |
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Abstract: | Purified platelet thrombospondin binds to immobilized fibrinogen if both Ca++ and Mg++ are present. Digestion of the purified molecule with thermolysin results in a limited number of discrete proteolytic fragments. When such digests are subjected to affinity chromatography on immobilized fibrinogen, only the fragments with Mr of 120,000 and 140,000 are specifically bound and subsequently eluted by the addition of EDTA to the column buffer. Examination by SDS-PAGE under both reducing and nonreducing conditions reveals that the fibrinogen-binding domain is derived from the region of the thrombospondin molecule containing the interchain disulfide bonds. The requirement for Ca++ and Mg++ for optimal binding to fibrinogen is also manifest by the Mr 120,000/140,000 thermolytic fragments. |
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Keywords: | To whom correspondence should be addressed at the Division of Laboratory Medicine. |
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