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ADP Initiates Phosphorylation Of Platelet Myosin Light Chain (MLC), A 40,000 Dalton Protein (40P) And Actin Binding Protein (ADP) Independent Of Secretion
1981
Thrombosis and Haemostasis
The mechanism by which ADP initiates platelet shape change and granule centralization is unknown. Recent studies of platelet proteins have provided evidence that raised intracellular calcium produces its effect by promoting protein phosphorylation. We have studied the influence of ADP on the phosphorylation of platelet proteins in both platelet rich plasma (PRP) and washed platelets, using the incorporation of 32p to identify phosphorylated proteins. 10u M ADP was found to cause a 2-5 fold
doi:10.1055/s-0038-1652234
fatcat:4tt74xvcefb3pc4mear56kypru