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.
Keywords: lipoxygenase, phagocyte, yeast two-hybrid, nadph oxidase, chaperone, dnak
Protein & Peptide Letters
Title: C-Terminus of p47phox Is Required for Interaction with Leukocyte Type Rat 12-Lipoxygenase
Volume: 12 Issue: 3
Author(s): Michiharu Tanabe, Hideki Kamitani, Takashi Watanabe and Olof Radmark
Affiliation:
Keywords: lipoxygenase, phagocyte, yeast two-hybrid, nadph oxidase, chaperone, dnak
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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Cite this article as:
Tanabe Michiharu, Kamitani Hideki, Watanabe Takashi and Radmark Olof, C-Terminus of p47phox Is Required for Interaction with Leukocyte Type Rat 12-Lipoxygenase, Protein & Peptide Letters 2005; 12 (3) . https://dx.doi.org/10.2174/0929866053587066
DOI https://dx.doi.org/10.2174/0929866053587066 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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