Biochemical evidence for heme linkage through esters with Asp-93 and Glu-241 in human eosinophil peroxidase. The ester with Asp-93 is only partially formed in vivo

The covalent heme attachment has been extensively studied by spectroscopic methods in myeloperoxidase and lactoperoxidase (LPO) but not in eosinophil peroxidase (EPO). We show that heme linkage to the heavy chain is invariably present, whereas heme linkage to the light chain of EPO is present in les...

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Veröffentlicht in:	The Journal of biological chemistry 1999-06, Vol.274 (24), p.16953-16958
Hauptverfasser:	Oxvig, C, Thomsen, A R, Overgaard, M T, Sorensen, E S, Højrup, P, Bjerrum, M J, Gleich, G J, Sottrup-Jensen, L
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Aspartic Acid - chemistry Chromatography, High Pressure Liquid Eosinophil Peroxidase Eosinophils - enzymology Esters Glutamic Acid - chemistry Heme - chemistry Humans Lactoperoxidase - chemistry Molecular Sequence Data Oligopeptides - chemistry Peroxidases - chemistry Sequence Analysis
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