| 牛白细胞髓过氧化物酶的分离纯化 |
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| 引用本文： | 石晶,吕英,杨宇,李庆章. 牛白细胞髓过氧化物酶的分离纯化[J]. 中国畜牧兽医, 2011, 38(5): 54-57 |
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| 作者姓名： | 石晶 吕英 杨宇 李庆章 |
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| 作者单位： | 东北农业大学乳品科学教育部重点实验室,黑龙江哈尔滨 150030 |
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| 基金项目： | "十一五"国家科技支撑计划重点项目 |
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| 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147.3 μg/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。
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| 关 键 词： | 奶牛 髓过氧化物酶 分离纯化 |
| 收稿时间： | 2010-10-15 |
Purification of Myeloperoxidase from White Blood Cells of Dairy Cow |
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| SHI Jing,LV Ying,YANG Yu,LI Qing-zhang. Purification of Myeloperoxidase from White Blood Cells of Dairy Cow[J]. China Animal Husbandry & Veterinary Medicine, 2011, 38(5): 54-57 |
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| Authors: | SHI Jing LV Ying YANG Yu LI Qing-zhang |
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| Affiliation: | Key Laboratory of Dairy Science,Ministry of Education,Northeast Agricultural University,Harbin 150030,China |
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| Abstract: | 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. |
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| Keywords: | dairy cow myeloperoxidase purification |
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