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Two conserved tryptophan residues of tumor necrosis factor and lymphotoxin are not involved in the biological activity
Author(s) -
Van Ostade Xaveer,
Tavernier Jan,
Fiers Walter
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80510-6
Subject(s) - lymphotoxin , tryptophan , lymphotoxin alpha , mutagenesis , site directed mutagenesis , phenylalanine , amino acid , mutant , biochemistry , chemistry , cytotoxicity , tumor necrosis factor alpha , biological activity , microbiology and biotechnology , biology , in vitro , immunology , gene , receptor
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.