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C-Terminus of p47phox Is Required for Interaction with Leukocyte Type Rat 12-Lipoxygenase

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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: chaperone; dnak; lipoxygenase; nadph oxidase; phagocyte; yeast two-hybrid

Document Type: Review Article


Affiliations: Department of Neurosurgery, Institute of Neurological Sciences, Faculty of Medicine, Tottori University, 36-1 Nishi-cho, Yonago City, 683-8504, Japan.

Publication date: April 1, 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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