FEBS Letters | |
Purification of the 28.5 kDa cytosolic protein involved in the activation of NADPH oxidase from guinea pig neutrophils | |
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 p47phox and p67phox, 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
【 预 览 】
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