ADP Causes Subsecond Changes in Protein Phosphorylation of Platelets
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چکیده
We developed a general quenched-flow approach to study platelet function as early as 0.3 seconds after stimulation. Phosphorylation of 20and 47-kiloDalton (kD) proteins was analyzed during the first 5 seconds of platelet response to ADP from 0.5 to 10.0 zmol/l and compared with the progress of aggregation. The onset time for aggregation and phosphorylation of both proteins was <1 second; 20-K phosphorylation was increased >200% and 47-K phosphorylation was increased 50%. The ADP sensitivity of 20-K phosphorylation was greater than that of 47-K phosphorylation (P < .025). and of that of aggregation (P < .01 ). with
منابع مشابه
ADP Causes Subsecond Changes in Protein Phosphorylation of Platelets
We developed a general quenched-flow approach to study platelet function as early as 0.3 seconds after stimulation. Phosphorylation of 20and 47-kiloDalton (kD) proteins was analyzed during the first 5 seconds of platelet response to ADP from 0.5 to 10.0 zmol/l and compared with the progress of aggregation. The onset time for aggregation and phosphorylation of both proteins was <1 second; 20-K p...
متن کاملADP causes subsecond changes in protein phosphorylation of platelets.
We developed a general quenched-flow approach to study platelet function as early as 0.3 seconds after stimulation. Phosphorylation of 20- and 47-kiloDalton (kD) proteins was analyzed during the first 5 seconds of platelet response to ADP from 0.5 to 10.0 mumol/L and compared with the progress of aggregation. The onset time for aggregation and phosphorylation of both proteins was less than 1 se...
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متن کاملThrombin causes subsecond changes in protein phosphorylation of platelets.
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تاریخ انتشار 2005