Isolation of the fibrinogen-binding region of platelet thrombospondin

Vishva M. Dixit, Gregory A. Grant, William A. Frazier, Samuel A. Santoro

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23 Scopus citations


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 additon 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.

Original languageEnglish
Pages (from-to)1075-1081
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Mar 30 1984


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