Giometti C S, Anderson N G
Clin Chem. 1984 Dec;30(12 Pt 1):2078-83.
Using two-dimensional electrophoresis, we mapped both the total and the cytoskeletal proteins of human platelets before and after activation with thrombin or the calcium ionophore A23187. Activation resulted in increased abundance of the phosphorylated form of myosin light chains with an approximate molecular mass of 20 kDa, decreased abundance of two proteins with molecular masses of approximately 18 and 25 kDa, and, in the case of activation with thrombin, the appearance of a new chain of protein spots (named "Thromb:1"). The latter, found associated with isolated detergent-insoluble cytoskeletons, reacted with antibody to human fibrinogen and thus were identified as gamma-gamma dimers of fibrin. The total number of proteins associated with the cytoskeleton increased after activation with either thrombin or A23187, but we observed some differences in which proteins were bound, and for how long.
我们使用二维电泳技术，绘制了人血小板在凝血酶或钙离子载体A23187激活前后的总蛋白和细胞骨架蛋白图谱。激活导致分子量约为20 kDa的肌球蛋白轻链磷酸化形式丰度增加，分子量约为18 kDa和25 kDa的两种蛋白丰度降低，并且在凝血酶激活的情况下，出现了一条新的蛋白斑点链（命名为“Thromb:1”）。后者与分离出的去污剂不溶性细胞骨架相关，与抗人纤维蛋白原抗体发生反应，因此被鉴定为纤维蛋白的γ-γ二聚体。用凝血酶或A23187激活后，与细胞骨架相关的蛋白总数增加，但我们观察到结合的蛋白种类以及结合时间存在一些差异。
