Abstract
The reaction of the β subunit of murine nerve growth factor (NGF) with diethylpyrocarbonate (DEP) results in the quantitative modification of histidine residues and the loss of binding to rabbit superior cervical ganglia microsomes. No conformational changes accompanied the conversion as judged by fluorescence spectra. Hydroxylamine converted the carbethoxy derivatives back to the unmodified imidazoles and simultaneously restored the capacity of NGF to bind to its receptor. Modification of des (1–9) NGF, from which His-4 and His-8 have been quantitatively removed, results in the same loss in binding activity, suggesting that His-75 and/or His-84 may play an important role in hormone-receptor interactions.
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Dunbar, J.C., Tregear, G.W. & Bradshaw, R.A. Histidine residue modification inhibits binding of murine β nerve growth factor to its receptor. J Protein Chem 3, 349–356 (1984). https://doi.org/10.1007/BF01025171
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DOI: https://doi.org/10.1007/BF01025171