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目的:考察半夏毒针晶刺激性毒性的稳定性及针晶蛋白对针晶刺激性毒性的贡献,为进一步揭示半夏毒针晶产生刺激性毒性的机制提供依据。方法:不同溶剂及混合蛋白酶液浸泡处理半夏及其毒针晶,用家兔眼结膜刺激性模型考察半夏及其所含针晶的刺激性变化,用电镜扫描法观察毒针晶晶体结构变化,采用垂直凝胶电泳(SDS-PAGE)试验分析蛋白酶液浸泡前后针晶蛋白的条带变化。结果:半夏毒针晶在甲醇、乙醇浸泡24 h内刺激性逐渐消失,半夏生品在75%乙醇溶液润制2 d后刺激性降低,扫描电镜显示经过甲醇、乙醇处理的毒针晶变得易于断碎,针尖锈蚀。混合蛋白酶液浸泡3 min后的半夏毒针晶刺激性急剧下降,SDS-PAGE图谱显示蛋白酶液浸泡后的针晶蛋白被酶解。结论:半夏针晶蛋白对针晶刺激性有贡献。甲醇、乙醇浸泡可使半夏毒针晶刺激性下降,提示可能是由于极性有机溶剂作用于针晶蛋白,逐渐破坏针晶蛋白的功能。
OBJECTIVE: To investigate the stability of pinellia stimulatory toxicity and the contribution of needle crystal to the ocular irritant toxicity of Pinellia spectabilis, so as to provide basis for further revealing the mechanism of pungent toxicity of pinellid needle. METHODS: Different solvents and mixed proteases were used to soak Pinellia ternata and its venom needle crystals. The conjunctival irritation model of rabbit eyes was used to investigate the stimulatory changes of Pinellia sinensis and its containing needles. The crystal structure was observed by SEM. Changes were analyzed using a vertical gel electrophoresis (SDS-PAGE) test to analyze changes in the band of the crystal protein before and after the protease solution was soaked. RESULTS: The stimulatory properties of Pinellia spectabilis disappeared after immersed in methanol and ethanol for 24 h. The pungent nature of Pinellia ternate was reduced after being treated with 75% ethanol for 2 days. Scanning electron microscopy showed that the needle crystals treated with methanol and ethanol became It is easy to break and the tip rusts. The stimulatory properties of Pinellia pinnatifida declined sharply after soaking in the mixed protein solution for 3 min. The SDS-PAGE pattern showed that the proteolytic solution of proteoglycan was digested by protease solution. Conclusion: Pinellia pinine has contributed to the stimulation of the needle crystal. Soaking in methanol and ethanol can reduce the irritating tingling ability of pinellia ternate. It may be due to the role of polar organic solvent in the growth of the needle crystal and gradually destroy the function of the pin crystal.