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[胆固醇羟化细胞色素P-450多肽链中四硝基甲烷修饰的酪氨酸残基的定位]

[Localization of tetranitromethane-modified tyrosine residues in the polypeptide chain of cholesterol-hydroxylating cytochrome P-450].

作者信息

Pikuleva I A, Lapko A G, Akhrem A A, Usanov S A, Chashchin V L

出版信息

Bioorg Khim. 1987 Jun;13(6):739-47.

PMID:3675633
Abstract

As a continuation of earlier structure-function relationship studies on cholesterol-hydroxylating cytochrome P-450 from the adrenal cortex mitochondria, the present study deals with the distribution of tetranitromethane-modified tyrosine residues in the hemeprotein polypeptide chain. Amino acid residues Tyr-24, -46, -50, -93, -94, -199, -246 are shown to be modified with tetranitromethane. Tyr-93, -94 are supposedly involved in the active site formation of cytochrome P-450.

摘要

作为早期对肾上腺皮质线粒体胆固醇羟化细胞色素P - 450结构 - 功能关系研究的延续,本研究探讨了四硝基甲烷修饰的酪氨酸残基在血红素蛋白多肽链中的分布。已证明氨基酸残基Tyr - 24、- 46、- 50、- 93、- 94、- 199、- 246被四硝基甲烷修饰。据推测,Tyr - 93、- 94参与细胞色素P - 450活性位点的形成。

相似文献

1
[Localization of tetranitromethane-modified tyrosine residues in the polypeptide chain of cholesterol-hydroxylating cytochrome P-450].[胆固醇羟化细胞色素P-450多肽链中四硝基甲烷修饰的酪氨酸残基的定位]
Bioorg Khim. 1987 Jun;13(6):739-47.
2
[Localization of tetranitromethane-modified tyrosine residues in domains of cholesterol-hydroxylating cytochrome P-450].
Bioorg Khim. 1984 Sep;10(9):1141-6.
3
[Selective chemical modification of cholesterol hydroxylating cytochrome P-450 from adrenal cortex mitochondria by tetranitromethane].[用四硝基甲烷对肾上腺皮质线粒体中胆固醇羟化细胞色素P-450进行选择性化学修饰]
Bioorg Khim. 1984 Jan;10(1):32-45.
4
[Primary structure of 20S,22R-cholesterol-hydroxylating cytochrome P-450 from bovine adrenal cortex mitochondria. IV. Structure of peptides of thermolytic and limited tryptic hydrolysis of the fragment F1; peptides of cyanogen bromide hydrolysis of cytochrome P-450. Complete amino acid sequence].[来自牛肾上腺皮质线粒体的20S,22R-胆固醇羟化细胞色素P-450的一级结构。IV. 片段F1的热解和有限胰蛋白酶水解肽段;细胞色素P-450的溴化氰水解肽段。完整氨基酸序列]
Bioorg Khim. 1985 Aug;11(8):1048-67.
5
[Primary structure of 20S,22R-cholesterol-hydroxylating cytochrome P-450 from bovine adrenal cortex mitochondria. Study of the structure of peptides obtained by hydrolysis of fragment F1 with proteinase from Staphylococcus aureus].
Bioorg Khim. 1985 Apr;11(4):455-70.
6
[The study of the active site of cytochrome P-450 LM2 using the chemical modification of tyrosine residues by tetranitromethane].[利用四硝基甲烷对酪氨酸残基进行化学修饰研究细胞色素P-450 LM2的活性位点]
Biokhimiia. 1984 Jun;49(6):889-98.
7
[Effect of chemical modification of tyrosine residues of cholesterol-hydroxylating cytochrome P-450 on the interaction with high-spin effectors].[胆固醇羟化细胞色素P-450酪氨酸残基化学修饰对与高自旋效应物相互作用的影响]
Biokhimiia. 1985 Jan;50(1):128-38.
8
[Chemical modification of cysteine residues of cholesterol-hydroxylating cytochrome P-450. Identification of the cysteine residue participating in the formation of a proximal ligand].
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9
[Primary structure of cholesterol-hydroxylating cytochrome P-450 from the mitochondria of the adrenal cortex in the bull].[公牛肾上腺皮质线粒体中胆固醇羟化细胞色素P-450的一级结构]
Dokl Akad Nauk SSSR. 1985;283(6):1510-2.
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[Separation of cholesterol-specific cytochrome P-450 regions and their localization in the polypeptide chain].
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