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- W2945168633 abstract "A fraction which competes with intact platelets for interaction with collagen was isolated from human platelets by Sepharose 2B-collagen (SC) affinity columns. Binding of platelets to SC columns, followed by lysis with a nonionic detergent and extensive wash with water (treated SC columns), reduced the columns’ capacity to subsequently bind platelets and induce serotonin release. This reduction was proportional to the number of platelets that had been applied to SC columns. Treated SC columns could be partially regenerated with solutions of high ionic strength (1 M NaCI or Tris-HCl) and most effectively with 0.3% sodium dodecylsulfate (SDS), but not with 8 M urea, 15% ethanol or 1% Triton X-100, indicating an ionic interaction. A fraction eluted with SDS from treated SC columns manifested receptor activity: when rebound to collagen it caused a dose-dependent decline in interaction of the collagen with intact platelets, as measured by binding and serotonin release. The receptor activity was sensitive to heat and was absorbed by an anionic exchange resin. When the membrane of intact platelets were labeled with 125I and lactoperoxidase, the derived receptor fraction contained a small proportion (about 1%) of the label." @default.
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- W2945168633 date "1977-01-01" @default.
- W2945168633 modified "2023-09-23" @default.
- W2945168633 title "Isolation of Platelet Membrane Collagen Receptor" @default.
- W2945168633 doi "https://doi.org/10.1055/s-0039-1680720" @default.
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