[HTML][HTML] Peroxynitrite-induced nitration of tyrosine hydroxylase: identification of tyrosines 423, 428, and 432 as sites of modification by matrix-assisted laser desorption …
DM Kuhn, M Sadidi, X Liu, C Kreipke, T Geddes… - Journal of Biological …, 2002 - ASBMB
Tyrosine hydroxylase (TH), the initial and rate-limiting enzyme in the biosynthesis of the
neurotransmitter dopamine, is inactivated by peroxynitrite. The sites of peroxynitrite-induced
tyrosine nitration in TH have been identified by matrix-assisted laser desorption time-of-flight
mass spectrometry and tyrosine-scanning mutagenesis. V8 proteolytic fragments of nitrated
TH were analyzed by matrix-assisted laser desorption time-of-flight mass spectrometry. A
peptide of 3135.4 daltons, corresponding to residues V410-E436 of TH, showed …
neurotransmitter dopamine, is inactivated by peroxynitrite. The sites of peroxynitrite-induced
tyrosine nitration in TH have been identified by matrix-assisted laser desorption time-of-flight
mass spectrometry and tyrosine-scanning mutagenesis. V8 proteolytic fragments of nitrated
TH were analyzed by matrix-assisted laser desorption time-of-flight mass spectrometry. A
peptide of 3135.4 daltons, corresponding to residues V410-E436 of TH, showed …