MONOCLONAL ANTIBODY-DIRECTED IMMUNOPURIFICATION AND IDENTIFICATION OF CYTOCHROMES-P-450
MONOCLONAL ANTIBODY-DIRECTED IMMUNOPURIFICATION AND IDENTIFICATION OF CYTOCHROMES-P-450
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DOI：
10.1016/s0006-291x(83)80221-6
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发表时间：
1983-01-01
影响因子：
3.1
通讯作者：
GELBOIN, HV
中科院分区：
文献类型：
--
作者：
FRIEDMAN, FK;ROBINSON, RC;GELBOIN, HV
用抗3-甲基胆蒽和苯巴比妥诱导的大鼠肝细胞色素P-450主要形式（分别为MC-P-450和PB-P-450）的单克隆抗体（MAb），用一步免疫吸附法对几种大鼠肝细胞色素P-450进行了纯化。当与溶解的大鼠肝微粒体混合时，基于抗MC-P-450的MAb的免疫吸附剂结合MW 56，000和57，000的2种多肽，而用抗PB-P-450的MAb制备的免疫吸附剂吸收MW 54，000的物质。这些多肽容易被0.1M甘氨酸（pH 3.0）解吸。通过这种方法分离MAb特异性细胞色素P-450同工酶在细胞色素P-450研究的许多阶段中具有应用。
Several rat liver cytochromes P-450 were substantially purified in a 1-step immunoadsorption procedure using Sepharose-bound monoclonal antibodies (MAb) to the major forms of rat liver cytochrome P-450 induced by 3-methylcholanthrene and phenobarbital (MC-P-450 and PB-P-450, respectively). When mixed with solubilized rat liver microsomes the immunoadsorbent based on the MAb to MC-P-450 binds 2 polypeptides of MW 56,000 and 57,000 while the immunoadsorbent made with the MAb to PB-P-450 absorbs a species of MW 54,000. These polypeptides are readily desorbed by 0.1 M glycine (pH 3.0). Isolation of MAb-specific cytochrome P-450 isozymes by this method has applications in numerous phases of cytochrome P-450 research.