Abstract
Differential screening-selected gene aberrative in neuroblastoma (DAN) encodes a protein which possesses metal binding motifs. Glutathione S-transferase DAN fusion protein had an ability to bind to Ni(2+)-immobilized affinity resin. Truncation of the C-terminal region including a (HX)n repeat of DAN caused a loss of binding ability to the affinity resin, suggesting that this region is essential for Ni(2+)-binding. DAN produced in cultured rat cells also had an affinity for Ni2+. Cross-linking experiments demonstrated that the C-terminal region might function as a protein-protein interacting domain.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Chromatography, Affinity
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Cross-Linking Reagents
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Genes, Tumor Suppressor
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Glutathione Transferase / biosynthesis
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Mammals
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Molecular Sequence Data
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Mutagenesis
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Nerve Tissue Proteins
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Neuroblastoma / genetics
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Neuroblastoma / metabolism
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Nickel / metabolism*
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Protein Binding
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Protein Biosynthesis
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Proteins / isolation & purification
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Proteins / metabolism*
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Rats
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Recombinant Fusion Proteins / biosynthesis
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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Sequence Deletion
Substances
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Cross-Linking Reagents
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Nbl1 protein, rat
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Nerve Tissue Proteins
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Proteins
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Recombinant Fusion Proteins
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Nickel
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Glutathione Transferase