Fig. 2.
Fig. 2. Immunodetection of myosin phosphatase in human platelets. Platelet lysates were immunoprecipitated with the antibody against MBS as described in the Materials and Methods. (A) Immunoprecipitates with anti-MBS antibody (a) or the preimmune serum (b) were immunoblotted with anti-MBS antibody. Immunoprecipitates with anti-MBS antibody were immunoblotted with antibodies against PP1δ catalytic subunit and the 20-kD subunit, respectively. The immunoprecipitate with the antibody against PP1δ catalytic subunit was immunoblotted with anti-MBS antibody. IP, immunoprecipitation antibody used; IB, immunoblotting antibody used; Ig, cross-reacted immunoglobulin. (B) Immunoprecipitates with anti-MBS antibody were assayed for phosphatase activity, using [32P]-MLC as substrate. Each phosphatase activity was determined in triplicate as described in Materials and Methods.

Immunodetection of myosin phosphatase in human platelets. Platelet lysates were immunoprecipitated with the antibody against MBS as described in the Materials and Methods. (A) Immunoprecipitates with anti-MBS antibody (a) or the preimmune serum (b) were immunoblotted with anti-MBS antibody. Immunoprecipitates with anti-MBS antibody were immunoblotted with antibodies against PP1δ catalytic subunit and the 20-kD subunit, respectively. The immunoprecipitate with the antibody against PP1δ catalytic subunit was immunoblotted with anti-MBS antibody. IP, immunoprecipitation antibody used; IB, immunoblotting antibody used; Ig, cross-reacted immunoglobulin. (B) Immunoprecipitates with anti-MBS antibody were assayed for phosphatase activity, using [32P]-MLC as substrate. Each phosphatase activity was determined in triplicate as described in Materials and Methods.

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