Swati Banger, Rita Singh, N. Tripathi, V. Pal, A. Goel
{"title":"One step Purification and Characterisation of Abrin Toxin from Abrus Precatorius Seeds","authors":"Swati Banger, Rita Singh, N. Tripathi, V. Pal, A. Goel","doi":"10.14429/dlsj.4.14967","DOIUrl":null,"url":null,"abstract":"Abrin is a plant toxin obtained from Abrus precatorius seeds. It belongs to the type II ribosomal inactivating proteins (RIPs) consisting of two chains namely, catalytically active A chain and sugar binding B chain linked by a single disulphide bond. Due to high toxicity of abrin, its exposure or consumption can lead to serious public health problems. In the present work, we have extracted and purified the abrin toxin from Abrus precatorius seeds. The toxin was purified using a single step anion exchange chromatography. The purified protein was characterized by SDS-PAGE and MALDI- TOF to confirm its purity. The toxicity of purified abrin toxin was also confirmed by injecting the toxin in mice. The purified protein was further used to raise antibodies in mice and characterized by indirect Enzyme Linked Immunosorbent Assay. The results of present study established the use of single step ion exchange chromatography to purify abrin toxin for further development of its detection system.","PeriodicalId":36557,"journal":{"name":"Defence Life Science Journal","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2019-10-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Defence Life Science Journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.14429/dlsj.4.14967","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"Pharmacology, Toxicology and Pharmaceutics","Score":null,"Total":0}
引用次数: 1
Abstract
Abrin is a plant toxin obtained from Abrus precatorius seeds. It belongs to the type II ribosomal inactivating proteins (RIPs) consisting of two chains namely, catalytically active A chain and sugar binding B chain linked by a single disulphide bond. Due to high toxicity of abrin, its exposure or consumption can lead to serious public health problems. In the present work, we have extracted and purified the abrin toxin from Abrus precatorius seeds. The toxin was purified using a single step anion exchange chromatography. The purified protein was characterized by SDS-PAGE and MALDI- TOF to confirm its purity. The toxicity of purified abrin toxin was also confirmed by injecting the toxin in mice. The purified protein was further used to raise antibodies in mice and characterized by indirect Enzyme Linked Immunosorbent Assay. The results of present study established the use of single step ion exchange chromatography to purify abrin toxin for further development of its detection system.