摘要
应用分子筛层析(Sephadex G-200凝胶)和亲和层析(ConA-Sephrose 4B)从奶牛全血中分离纯化髓过氧化物酶(myeloperoxidase,MPO)。分离出的MPO活性为0.068 U/mL,分子质量为64.7、47.9、13.4 ku,纯度为94.2%,蛋白质浓度为147.3μg/mL。本研究建立了MPO分离纯化方法,对于深入研究MPO具有重要意义。
The protein myeloperoxidase（MPO） was isolated and purified from bovine whole blood by Sephadex G-200 chromatography and ConA-Sephrose 4B affinity chromatography.The activity,molecular weight,rate of purity and protein concentration of MPO were 0.068 U/mL,64.7,47.9,13.4 ku,94.2% and 147.3 μg/mL,respectively.The method developed for the isolation and purification of MPO was important for the following research.
出处
《中国畜牧兽医》
CAS
北大核心
2011年第5期54-57,共4页
China Animal Husbandry & Veterinary Medicine
基金
"十一五"国家科技支撑计划重点项目"国家重点领域认证认可推进工程"(2008BAK42B05)
