Fig. 4.
Fig. 4. Immunoprecipitation of 6 different proteolytic fragments of GPIb. / Surface-biotinylated mouse platelets were incubated for 6 hours at RT and lysed directly. Immunoprecipitation was performed with p0p 1,3,4,5 and control IgG1. Proteins were separated by 9% to 15% SDS-PAGE under reducing conditions and were detected by streptavidin-HRP/ECL. (right) Schematic drawing of the murine GPIb-IX complex. (arrows ) Proposed cleavage sites (1, 2, 3). (left, arrows) Assumed binding sites of p0p 1-5. (middle) Schematic drawing of fragment pairs shown on the blot.

Immunoprecipitation of 6 different proteolytic fragments of GPIb.

Surface-biotinylated mouse platelets were incubated for 6 hours at RT and lysed directly. Immunoprecipitation was performed with p0p 1,3,4,5 and control IgG1. Proteins were separated by 9% to 15% SDS-PAGE under reducing conditions and were detected by streptavidin-HRP/ECL. (right) Schematic drawing of the murine GPIb-IX complex. (arrows ) Proposed cleavage sites (1, 2, 3). (left, arrows) Assumed binding sites of p0p 1-5. (middle) Schematic drawing of fragment pairs shown on the blot.

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