ROLE OF A HYDROPHOBIC POLYPEPTIDE IN THE N-TERMINAL REGION OF NADPH-CYTOCHROME P-450 REDUCTASE IN COMPLEX-FORMATION WITH P-450LM
ROLE OF A HYDROPHOBIC POLYPEPTIDE IN THE N-TERMINAL REGION OF NADPH-CYTOCHROME P-450 REDUCTASE IN COMPLEX-FORMATION WITH P-450LM
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DOI：
10.1016/0006-291x(79)91238-5
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发表时间：
1979-01-01
影响因子：
3.1
通讯作者：
COON, MJ
中科院分区：
文献类型：
--
作者：
BLACK, SD;FRENCH, JS;COON, MJ
洗涤剂溶解的肝微粒体NADPH-细胞色素P-450还原酶保留了催化电子转移到细胞色素P-450的能力，而胰蛋白酶溶解的还原酶则没有。用胰蛋白酶处理高度纯化的洗涤剂溶解的兔肝酶（MW 77，700），显示出产生一种小肽（MW 6100）以及保留黄素辅基的大肽（MW 71，200）。如其氨基酸组成和溶解度性质所示，小肽本质上是疏水性的，显然是天然还原酶中参与与细胞色素P-450和微粒体膜结合的部分。天然还原酶和大片段的C-末端氨基酸序列相同[-Trp-（Leu，瓦尔）-Asp-Ser-COOH]，表明疏水肽位于酶的N-末端区域。
Detergent-solubilized liver microsomal NADPH-cytochrome P-450 reductase retains the ability to catalyze electron transfer to cytochrome P-450, whereas the trypsin-solubilized reductase does not. Treatment of the highly purified detergent-solubilized rabbit liver enzyme (MW 77,700) with trypsin was shown to yield a small peptide (MW 6100) as well as the large peptide (MW 71,200) which retains the flavin prosthetic groups. The small peptide, which is hydrophobic in nature as shown by its amino acid composition and solubility properties, is apparently the moiety in the native reductase involved in binding to cytochrome P-450 and to the microsomal membrane. The C-terminal amino acid sequences of the native reductase and large fragment are identical [-Trp-(Leu, Val)-Asp-Ser-COOH], indicating that the hydrophobic peptide is located in the N-terminal region of the enzyme.