Association of membrane and cytoplasmic proteins with the cytoskeleton in blood platelets.
Association of membrane and cytoplasmic proteins with the cytoskeleton in blood platelets.
复制标题
膜和细胞质蛋白与血小板中细胞骨架的关联。
DOI：
10.1021/bi00537a002
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发表时间：
1982
期刊：
影响因子：
2.9
通讯作者：
S. Linder
中科院分区：
文献类型：
--
作者：
A. Rotman;J. Heldman;S. Linder
研究了静息血小板和活化血小板的细胞骨架与膜蛋白和胞浆蛋白的关系。用125 I标记的凝集素（伴刀豆球蛋白A、麦胚凝集素和透镜culinaris）标记糖蛋白。多肽，这是嵌入在脂质双分子层，已确定其光标记与脂溶性试剂5-[125 I]碘萘1-叠氮（125 INA）。胞质蛋白质通过其与胞内探针叠氮荧光素二乙酸酯的光标记来鉴定。结果表明，Triton X-100残基含有膜结合糖蛋白Ia，一个95 000-道尔顿的蛋白质，和另外两个酸性蛋白，分子量为35 000-40 000，一个用125 INA标记，另一个用叠氮荧光素二乙酸酯标记。Triton残基中这些蛋白质的部分存在取决于血小板活化的模式。糖蛋白IIb和III嵌入膜脂双层中，但仅在凝血酶活化后与Triton残基一起沉淀。另一种Mr为70 000的蛋白质仅在Triton可溶性部分中发现，该蛋白质在静息血小板中被125 INA高度标记。
The association of membrane and cytoplasmic proteins with the cytoskeleton of resting and activated platelets was studied. Glycoproteins were identified by labeling with 125I-labeled lectins (concanavalin A, wheat germ agglutinin, and Lens culinaris). Polypeptides, which are embedded in the lipid bilayer, have been identified by their photolabeling with the lipid-soluble reagent 5-[125I]iodonaphthyl 1-azide (125INA). Cytoplasmic proteins were identified by their photolabeling with the intracellular probe azidofluorescein diacetate. Results indicate that the Triton X-100 residue contains the membrane-associated glycoprotein Ia, a 95 000-dalton protein, and two other acidic proteins of molecular weights of 35 000-40 000, one labeled with 125INA and the other with azidofluorescein diacetate. The presence of part of these proteins in the Triton residue is dependent upon the mode of platelet activation. Glycoproteins IIb and III are embedded in the membrane lipid bilayer but sedimented with the Triton residue only after thrombin activation. Another protein with Mr 70 000, which is highly labeled by 125INA in resting platelets, is found only in the Triton-soluble fraction.