A cDNA encoding rat p47phox was cloned from rat spleen cDNA library, utilizing rapid amplification of cDNA ends. The open reading frame corresponded to 389 amino acids: It contained the phagocyte oxidase homology domain, two Src homology 3 domains and a proline rich region, all of which are conserved in mammalian p47phox sequences. Rat p47phox displayed the highest degree of identity to mouse p47phox (94%). We expressed and purified rat p41phox as a glutathione S-transferase fusion protein, and found that the rat protein could replace human p47 phox in a cell-free activation system for human NADPH oxidase, giving about half activity. Although rat 12-lipoxygenase interacted with human p47phox in a yeast two-hybrid system, this was not the case for rat p47phox.
|Number of pages||4|
|Journal||DNA Sequence - Journal of DNA Sequencing and Mapping|
|Publication status||Published - Feb 2005|
All Science Journal Classification (ASJC) codes
- Molecular Biology