[Purification and characterization of trichokirin-S1, a novel ribosome-inactivating peptide from seeds of Trichosanthes kirilowii].

Feng Li, Xin-Xiu Yang, Wei-Guo Hu, Hen-Chuan Xia, Zhen Li, Zu-Chuan Zhang
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引用次数: 0

Abstract

A novel peptide from the seeds of Trichosanthes kirilowii, trichokirin-S1, was purified by extraction of protein body, ammonia sulfate precipitation, Blue-gel affinity chromatography, FPLC Mono S ion exchange chromatography and Superose12 gel filtration chromatography. Its molecular weight was determined to be 11,426 by MALDI-TOF MS analysis. Its reaction mechanism to inactive ribosome was the same as that of the ribosome-inactivating protein trichosanthin, a rRNA N-glycosidase. The purified trichokirin-S1 showed a strong inhibitory activity on protein synthesis in cell-free rabbit reticulocyte lysate system, with IC(50) of 0.7 nmol/L. Therefore, trichokirin-S1 may be a promising and efficient toxin moiety of immunotoxins.

[一种新型核糖体失活肽trichokirin-S1的纯化和鉴定]。
采用蛋白体提取、硫酸氨沉淀法、蓝凝胶亲和层析、FPLC Mono S离子交换层析和Superose12凝胶过滤层析等方法纯化了栝蚕种子中的新多肽trichokirin-S1。通过MALDI-TOF质谱分析确定其分子量为11426。其对失活核糖体的反应机制与核糖体失活蛋白trichosanthin(一种rRNA n -糖苷酶)相同。纯化后的trichokirin-S1对无细胞兔网织细胞裂解体系中蛋白质合成有较强的抑制活性,IC(50)为0.7 nmol/L。因此,trichokirin-S1可能是一种很有前途的高效免疫毒素。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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