Chow T W, McIntire L V, Peterson D M
Biochim Biophys Acta. 1985 Jan 25;812(2):512-22. doi: 10.1016/0005-2736(85)90326-8.
Concanavalin A was employed to study the role of platelet membrane glycoproteins in platelet-fibrin interactions during clot formation. A rheological technique was used to study the interactions, measuring the clot rigidity and platelet contractile force simultaneously during the formation of network structure. Concanavalin A lowered the clot rigidity and contractile force of a platelet-rich plasma clot by a small extent. Plasma glycoproteins probably compete with platelet membranes for concanavalin A binding in platelet-rich plasma. Both native concanavalin A (tetrameric) and succinyl concanavalin A (dimeric) lowered the clot rigidity and contractile force of a washed platelet-fibrin clot dramatically, almost down to those values found for fibrin clots. Inhibition studies with alpha-methyl-D-mannoside indicated that the concanavalin A effects were specific for the concanavalin A binding capacity to platelets. The effects of native concanavalin A on platelet-fibrin clots were only partially reversible, while the succinyl concanavalin A effects were completely reversible. The observed concanavalin A effects are probably mainly due to concanavalin A binding to platelet membrane glycoproteins. The concanavalin A binding site appears to play an important role in the fibrin binding to platelets.
刀豆球蛋白A被用于研究血小板膜糖蛋白在血凝块形成过程中血小板-纤维蛋白相互作用中的作用。采用流变学技术研究这些相互作用，在网络结构形成过程中同时测量血凝块硬度和血小板收缩力。刀豆球蛋白A在一定程度上降低了富含血小板血浆凝块的硬度和收缩力。血浆糖蛋白可能在富含血小板血浆中与血小板膜竞争刀豆球蛋白A的结合。天然刀豆球蛋白A（四聚体）和琥珀酰刀豆球蛋白A（二聚体）都显著降低了洗涤过的血小板-纤维蛋白凝块的硬度和收缩力，几乎降至纤维蛋白凝块的相应值。用α-甲基-D-甘露糖苷进行的抑制研究表明，刀豆球蛋白A的作用对其与血小板的结合能力具有特异性。天然刀豆球蛋白A对血小板-纤维蛋白凝块的作用仅部分可逆，而琥珀酰刀豆球蛋白A的作用则完全可逆。观察到的刀豆球蛋白A的作用可能主要归因于其与血小板膜糖蛋白的结合。刀豆球蛋白A结合位点似乎在纤维蛋白与血小板的结合中起重要作用。
