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尖吻蝮蛇毒中抗血小板凝集素是凝血因子IX/凝血因子X结合蛋白,它具有抗凝血和抑制血小板凝集双重活性。用红外光谱、拉曼光谱和CD谱研究了抗血小板凝集素的二级结构以及pH值和钙离子对其二级结构的影响。用CD谱测得,在水溶液中,抗血小板凝集素的主要骨架构象为β-折叠(26.3%)和α-螺旋(19.6%)结构。拉曼光谱显示,在粉末状态,其α-螺旋含量显著降低。CD谱还表明,抗血小板凝集素在pH值3.0￣11.0范围内保持稳定的天然结构,钙离子诱导的抗血小板凝集素结构变化是可逆的,钙离子在稳定抗血小板凝集素的天然结构中起重要作用。
Agkistrodon acutus venom anti-platelet agglutinin is a factor IX / factor X binding protein, which has anti-coagulation and inhibition of platelet aggregation dual activity. The secondary structure of anti-platelet lectin and the effect of pH value and calcium ion on its secondary structure were studied by IR, Raman and CD spectra. The main skeletal conformation of anti-platelet agglutinin in aqueous solution was β-sheet (26.3%) and α-helix (19.6%) as determined by CD spectroscopy. Raman spectroscopy showed that the α-helix content was significantly reduced in the powder state. The CD spectra also show that anti-platelet agglutinin maintains a stable native structure at a pH of 3.0-11.0, that calcium-induced structural changes in anti-platelet lectin are reversible, that calcium ions play a role in stabilizing the natural structure of anti-platelet agglutinin Important role.