Purification of the 28.5 kDa cytosolic protein involved in the activation of NADPH oxidase from guinea pig neutrophils

FEBS Letters

Nagaoka, Isao¹  Yomogida, Shin¹  Iwabuchi, Kazuhisa¹  Someya, Akimasa¹  Yamashita, Tatsuhisa¹ 

[1] Department of Biochemistry, Juntendo University, School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113, Japan

关键词: Cytosolic factor;    NADPH oxidase;    Superoxide production;    Neutrophil;    Cell-free system;    p47phox;    47 kDa cytosolic phagocyte oxidase component;    p67phox;    67 kDa cytosolic phagocyte oxidase component;   

DOI  :  10.1016/0014-5793(92)80287-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We tried to purify a new protein component required for the activation of NADPH oxidase from the guinea pig neutrophil cytosolic fraction which did not contain p47^phox and p67^phox, using HAC-5CP, IEC-QA and Superose 12HR columns. The NADPH oxidase-activating activity was separated into three fractions on IEC-QA anion-exchange HPLC. However, when each of the fractions was purified by Superose 12HR gel filtration, the active fraction eluted at the same position, and was found to contain a common protein with a molecular weight of 28.5 kDa on SDS-PAGE. These results suggest that the 28.5 kDa protein is a novel NADPH oxidase activating protein.

【 授权许可】

Unknown