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  • Title: Affinity modulation in platelet alpha 2 beta 1 following ligand binding.
    Author: Gofer-Dadosh N, Klepfish A, Schmilowitz H, Shaklai M, Lahav J.
    Journal: Biochem Biophys Res Commun; 1997 Mar 27; 232(3):724-7. PubMed ID: 9126343.
    Abstract:
    In order to test for ligand-induced change in the affinity of platelet alpha 2 beta 1 to collagen we passaged labeled viable platelets through a column of fibrillar collagen and used stringent lysis conditions to remove all low-affinity receptors. A high affinity fraction left on the collagen could be eluted with DTT and 2% SDS. Antibodies raised against it Western-blotted alpha 2 beta 1. Functional tests performed with the antibodies confirmed the involvement of the high affinity proteins in platelet-collagen interactions attributed to alpha 2 beta 1: inhibition of collagen-specific platelet adhesion and aggregation. EDTA, chaotropic agents or low pH did not elute the high affinity fraction of alpha 2 beta 1. However, DTT followed by acetic acid did. Our data suggest that 1) ligand binding induces the formation of a new disulfide bond in a fraction of alpha 2 beta 1, 2) that this bond is intrareceptor and 3) that this change increases the affinity of the receptor to its ligand.
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