Ingelman-Sundberg M, Jörnvall H
Biochem Biophys Res Commun. 1984 Oct 30;124(2):375-82. doi: 10.1016/0006-291x(84)91563-8.
Cytochrome P-450 LMeb was purified from liver microsomes obtained from rabbits treated with either benzene or imidazole and was shown to have identical N-terminal amino acid sequence as that of cytochrome P-450 LM3a. The amino acid compositions of the proteins were indistinguishable. Quantitation of P-450 LMeb in various types of microsomes using radial immunodiffusion, revealed that pyrazole- or imidazole-treatment of the animals caused a 2-3-fold induction of the enzyme, accompanied by 2-3-fold increases of the rates of ethanol and aniline oxidation.
细胞色素P-450 LMeb是从用苯或咪唑处理过的兔子的肝脏微粒体中纯化得到的，结果显示其N端氨基酸序列与细胞色素P-450 LM3a的完全相同。这两种蛋白质的氨基酸组成无法区分。使用放射免疫扩散法对各种微粒体中的P-450 LMeb进行定量分析，结果表明用吡唑或咪唑处理动物会使该酶诱导增加2至3倍，同时乙醇和苯胺氧化速率也提高2至3倍。
