人中性粒细胞中依赖NADPH的产氧氧化酶的分离黄素蛋白和细胞色素B组分的催化特性。

Catalytic properties of the resolved flavoprotein and cytochrome B components of the NADPH dependent O2- . generating oxidase from human neutrophils.

作者信息

Gabig T G, Lefker B A

出版信息

Biochem Biophys Res Commun. 1984 Jan 30;118(2):430-6. doi: 10.1016/0006-291x(84)91321-4.

Abstract

The resolved flavoprotein and cytochrome b559 components of the NADPH dependent O2- . generating oxidase from human neutrophils were the subject of further study. The resolved flavoprotein, depleted of cytochrome b559, was reduced by NADPH under anaerobic conditions and reoxidized by oxygen. NADPH dependent O2- . generation by the resolved flavoprotein fraction was not detectable, however it was competent in the transfer of electrons from NADPH to artificial electron acceptors. The resolved cytochrome b559, depleted of flavoprotein, demonstrated no measureable NADPH dependent O2- . generating activity and was not reduced by NADPH under anaerobic conditions. The dithionite reduced form of the resolved cytochrome b559 was rapidly oxidized by oxygen, as was the cytochrome b559 in the intact oxidase.

摘要

人中性粒细胞中依赖NADPH的产O₂⁻氧化酶的已分离黄素蛋白和细胞色素b559组分成为了进一步研究的对象。已分离的、不含细胞色素b559的黄素蛋白在厌氧条件下被NADPH还原，并被氧气再氧化。已分离的黄素蛋白组分依赖NADPH的O₂⁻生成无法检测到，然而它能够将电子从NADPH转移至人工电子受体。已分离的、不含黄素蛋白的细胞色素b559未表现出可测量的依赖NADPH的O₂⁻生成活性，且在厌氧条件下不被NADPH还原。已分离的细胞色素b559的连二亚硫酸盐还原形式被氧气迅速氧化，完整氧化酶中的细胞色素b559也是如此。