Deconstruction of Activity-Dependent Covalent Modification of Heme in Human Neutrophil Myeloperoxidase by Multistage Mass Spectrometry (MS4)

Myeloperoxidase (MPO) is known to be inactivated and covalently modified by treatment with hydrogen peroxide and agents similar to 3-(2-ethoxypropyl)-2-thioxo-2,3-dihydro-1H-purin-6(9H)-one (1), a 254.08 Da derivative of 2-thioxanthine. Peptide mapping by liquid chromatography and mass spectrometry...

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Veröffentlicht in:	Biochemistry (Easton) 2012-03, Vol.51 (10), p.2065-2077
Hauptverfasser:	Geoghegan, Kieran F, Varghese, Alison H, Feng, Xidong, Bessire, Andrew J, Conboy, James J, Ruggeri, Roger B, Ahn, Kay, Spath, Samantha N, Filippov, Sergey V, Conrad, Steven J, Carpino, Philip A, Guimarães, Cristiano R. W, Vajdos, Felix F
Format:	Artikel
Sprache:	eng
Schlagworte:	08 HYDROGEN Amino Acid Sequence ATOMS Catalytic Domain CHROMATOGRAPHY Chromatography, Liquid Crystallography, X-Ray DISSOCIATION ENZYMES HEME Heme - chemistry Humans HYDROGEN HYDROGEN PEROXIDE IRON ISOTOPES MASS SPECTROSCOPY Models, Chemical Models, Molecular MODIFICATIONS Molecular Sequence Data Molecular Weight NEUTROPHILS Neutrophils - enzymology ORIENTATION Oxidation-Reduction Peptide Fragments - chemistry Peptide Mapping PEPTIDES Peroxidase - chemistry Peroxidase - metabolism POLYPEPTIDES PRECURSOR PYRROLES SPECTROMETERS SULFUR Tandem Mass Spectrometry
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