{"title":"从寄主植物中分离的、用抗病毒糖蛋白预处理的、从Boerhaavia diffusia植物根中分离的抗病毒蛋白的分子特征","authors":"Sharma Nk, Awasthi Lp","doi":"10.15406/JHVRV.2017.05.00156","DOIUrl":null,"url":null,"abstract":"Antiviral proteins were isolated, from host plants, following treatment with an antiviral glycoprotein, extracted from the roots of Boerhaavia diffusa plants. It was found to be active against isometric as well as an isometric viruses in their respective hypersensitive and systemic hosts. The biologically active principal was isolated and purified. Estimation of proteins, from the leaf samples of N.glutinosa plants, indicated higher concentration of new proteins in plants whose two basal leaves were treated 24 hours earlier with an aqueous solution of the glycoprotein. SDS-PAGE analysis studies on partially purified antiviral principal of protein nature revealed that the size of band in L3 (after 24 hours) was 30 Kda along with very dark and prominent bands. The size of band recorded in rest treatments was of 36 Kda and 50 Kda.","PeriodicalId":92670,"journal":{"name":"Journal of human virology & retrovirology","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2017-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"5","resultStr":"{\"title\":\"Molecular Characterization of Antiviral Proteins, Isolated from Host Plants, Pretreated with Antiviral Glycoprotein, Isolated from Roots of Boerhaavia Diffusa Plants\",\"authors\":\"Sharma Nk, Awasthi Lp\",\"doi\":\"10.15406/JHVRV.2017.05.00156\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Antiviral proteins were isolated, from host plants, following treatment with an antiviral glycoprotein, extracted from the roots of Boerhaavia diffusa plants. It was found to be active against isometric as well as an isometric viruses in their respective hypersensitive and systemic hosts. The biologically active principal was isolated and purified. Estimation of proteins, from the leaf samples of N.glutinosa plants, indicated higher concentration of new proteins in plants whose two basal leaves were treated 24 hours earlier with an aqueous solution of the glycoprotein. SDS-PAGE analysis studies on partially purified antiviral principal of protein nature revealed that the size of band in L3 (after 24 hours) was 30 Kda along with very dark and prominent bands. The size of band recorded in rest treatments was of 36 Kda and 50 Kda.\",\"PeriodicalId\":92670,\"journal\":{\"name\":\"Journal of human virology & retrovirology\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2017-04-04\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of human virology & retrovirology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.15406/JHVRV.2017.05.00156\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of human virology & retrovirology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15406/JHVRV.2017.05.00156","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Molecular Characterization of Antiviral Proteins, Isolated from Host Plants, Pretreated with Antiviral Glycoprotein, Isolated from Roots of Boerhaavia Diffusa Plants
Antiviral proteins were isolated, from host plants, following treatment with an antiviral glycoprotein, extracted from the roots of Boerhaavia diffusa plants. It was found to be active against isometric as well as an isometric viruses in their respective hypersensitive and systemic hosts. The biologically active principal was isolated and purified. Estimation of proteins, from the leaf samples of N.glutinosa plants, indicated higher concentration of new proteins in plants whose two basal leaves were treated 24 hours earlier with an aqueous solution of the glycoprotein. SDS-PAGE analysis studies on partially purified antiviral principal of protein nature revealed that the size of band in L3 (after 24 hours) was 30 Kda along with very dark and prominent bands. The size of band recorded in rest treatments was of 36 Kda and 50 Kda.