{"title":"Evaluation of in vitro Anti-proliferative Activity of L-arginine deiminase from Novel Marine Bacterial Isolate","authors":"Rahamat Unissa, M. Sudhakar, A. Reddy","doi":"10.9734/BMRJ/2016/23592","DOIUrl":null,"url":null,"abstract":"L-Arginine deiminase is a therapeutic l-arginine depleter found to counteract various arginine auxotrophic cancer cells (do not express ASS/OCT). The aim of the present study was to evaluate the anti -proliferative activity of the purified l-arginine deiminase from Vibrio alginolyticus 1374. Production of the enzyme was carried out by shake flask method under optimal conditions. The enzyme thus produced was purified to near homogeneity by ammonium sulphate fractionation followed by ion exchange and gel filtration chromatography. The enzyme was purified to 529.43 fold and showed final specific activity of 280.6 IU/mg with 43.5% yield. SDS-PAGE revealed that Original Research Article","PeriodicalId":9269,"journal":{"name":"British microbiology research journal","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"3","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"British microbiology research journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.9734/BMRJ/2016/23592","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 3
Abstract
L-Arginine deiminase is a therapeutic l-arginine depleter found to counteract various arginine auxotrophic cancer cells (do not express ASS/OCT). The aim of the present study was to evaluate the anti -proliferative activity of the purified l-arginine deiminase from Vibrio alginolyticus 1374. Production of the enzyme was carried out by shake flask method under optimal conditions. The enzyme thus produced was purified to near homogeneity by ammonium sulphate fractionation followed by ion exchange and gel filtration chromatography. The enzyme was purified to 529.43 fold and showed final specific activity of 280.6 IU/mg with 43.5% yield. SDS-PAGE revealed that Original Research Article
京公网安备 11010802042870号
京ICP备2023020795号-1
分享
求助内容：
应助结果提醒方式：
扫码关注我们
