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首页> 外文期刊>Biochemistry >Phosphorylation of Native and heme-Modified CYP3A4 by Protein Kinase C: A Mass spectrometric characterization of the phosphorylated peptides
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Phosphorylation of Native and heme-Modified CYP3A4 by Protein Kinase C: A Mass spectrometric characterization of the phosphorylated peptides

机译:天然蛋白和血红素修饰的CYP3A4被蛋白激酶C磷酸化:磷酸化肽段的质谱表征

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摘要

As an initial approach toward the characterization of the phosphorylation of cumene hydroperoxide (CuOOH)-inactivated cytochrome P450 (CYP3A4, the major human liver drug-metabolizing enzyme) and its role in the degradation of the inactivated protein, we have identified one of the major participating cytosolic kinase(s) as rat liver cytosolic protein kinase C (PKC) with the use of specific and general kinase inhibitors.
机译:作为表征氢过氧化枯烯(CuOOH)灭活的细胞色素P450(CYP3A4,主要的人肝药物代谢酶)的磷酸化及其在灭活蛋白降解中的作用的初步方法,我们确定了一种主要方法使用特定和一般的激酶抑制剂参与作为大鼠肝细胞溶质蛋白激酶C(PKC)的参与性胞质激酶。

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