Purification of bovine hemoglobin via fast performance liquid chromatography
Purification of bovine hemoglobin via fast performance liquid chromatography
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DOI：
10.1016/j.jchromb.2007.05.040
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发表时间：
2007-09-01
影响因子：
3
通讯作者：
Palmer, Andre F.
中科院分区：
文献类型：
--
作者：
Dimino, Michael L.;Palmer, Andre F.
牛血红蛋白（bHb）是通过阴离子交换色谱法从牛红细胞（bRBC）中纯化出来的。这是一种使用Q Sepharose XL（一种强阴离子交换树脂）从bRBC中获得bHb的快速有效方法。该树脂的结合能力为bHb的两倍相比，其他三种阴离子交换树脂，在这项工作中进行了研究。高铁血红蛋白水平保持在2%以下，bHb浓度在0.7和1.7 mM之间。通过SDS-PAGE和尺寸排阻色谱法（SEC）证实了bHb的高纯度。(C)2007 Elsevier B. V.保留所有权利。
Bovine hemoglobin (bHb) was purified from bovine red blood cells (bRBCs) via anion exchange chromatography preceded by dialysis. This is a fast and effective way to obtain bHb,from bRBCs using Q Sepharose XL, a strong anion exchange resin. This resin had double the binding capacity for bHb compared to three other anion exchange resins that were studied in this work. Methemoglobin levels remained below 2% with bHb concentrations between 0.7 and 1.7 mM. The high purity of bHb was confirmed via SDS-PAGE and size exclusion chromatography (SEC). (C) 2007 Elsevier B.V. All rights reserved.