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2000
Volume 12, Issue 3
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

In yeast two-hybrid system, rat 12-lipoxygenase (12-LO) bound to complete (390 amino acids) or the Nterminus truncated form of human p47 phox, but not to the C-terminus truncated form (residues 1-286). When glutathione S-transferase fused human p47phox was added to an in vitro 12-LO enzyme activity assay, formation of 12- hydroperoxyeicosatetraenoic acid was reduced significantly compared to the C-terminus truncated form. These results indicate that C-terminus of p47phox is important for its interaction to rat 12-LO.

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/content/journals/ppl/10.2174/0929866053587066
2005-04-01
2025-05-22
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/content/journals/ppl/10.2174/0929866053587066
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  • Article Type:
    Review Article
Keyword(s): chaperone; dnak; lipoxygenase; nadph oxidase; phagocyte; yeast two-hybrid
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