Abstract
Each of the two highly conserved tryptophan residues in hTNF (positions 28 and 114) was converted into phenylalanine by site-directed mutagenesis and the mutant proteins were partially purified. A cytotoxicity assay on mouse L929 cells showed only a slight reduction in biological activity, strongly suggesting that neither of the two amino acids is involved in the active site.
Publication types
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Comparative Study
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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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Base Sequence
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Binding Sites
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Cell Survival
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Cloning, Molecular
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DNA / genetics
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DNA, Recombinant
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Escherichia coli / genetics
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Humans
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Lymphotoxin-alpha / genetics
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Lymphotoxin-alpha / metabolism*
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Mice
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Molecular Sequence Data
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Mutation
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Phenylalanine
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Plasmids
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Structure-Activity Relationship
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Transformation, Genetic
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Tryptophan*
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Tumor Necrosis Factor-alpha / genetics
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Tumor Necrosis Factor-alpha / physiology*
Substances
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DNA, Recombinant
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Lymphotoxin-alpha
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Tumor Necrosis Factor-alpha
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Phenylalanine
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Tryptophan
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DNA