{"title":"[一种新型核糖体失活肽trichokirin-S1的纯化和鉴定]。","authors":"Feng Li, Xin-Xiu Yang, Wei-Guo Hu, Hen-Chuan Xia, Zhen Li, Zu-Chuan Zhang","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":21763,"journal":{"name":"Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica","volume":"35 9","pages":"841-6"},"PeriodicalIF":0.0000,"publicationDate":"2003-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Purification and characterization of trichokirin-S1, a novel ribosome-inactivating peptide from seeds of Trichosanthes kirilowii].\",\"authors\":\"Feng Li, Xin-Xiu Yang, Wei-Guo Hu, Hen-Chuan Xia, Zhen Li, Zu-Chuan Zhang\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>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.</p>\",\"PeriodicalId\":21763,\"journal\":{\"name\":\"Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica\",\"volume\":\"35 9\",\"pages\":\"841-6\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2003-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
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。
[Purification and characterization of trichokirin-S1, a novel ribosome-inactivating peptide from seeds of Trichosanthes kirilowii].
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.