Evidence for and partial characterization of three major and three minor chromatographic forms of human neutrophil myeloperoxidase

• Published in: Archives of biochemistry and biophysics Vol. 246; no. 2; pp. 751 - 764
• Main Authors: Miyasaki, Kenneth T., Wilson, Mark E., Cohen, Elias, Jones, Pamela C., Genco, Robert J.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 01.05.1986; Elsevier
• Subjects: Amino Acids - blood; Amitrole - pharmacology; Animals; Applied sciences; Azides; Cattle; Cetrimonium; Cetrimonium Compounds; Chromatography - methods; Chromatography, Liquid - methods; Electrophoresis, Polyacrylamide Gel; Exact sciences and technology; Hexosamines - analysis; Humans; Immunoelectrophoresis, Two-Dimensional; Lactoperoxidase; Milk - enzymology; Neutrophils - enzymology; Other techniques and industries; Peroxidase - antagonists & inhibitors; Peroxidase - blood; Sodium Azide; Spectrophotometry

Myeloperoxidase (MPO) is an enzyme found in the azurophil granules of neutrophils. Cation-exchange chromatography on carboxymethyl-cellulose previously has been used to demonstrate the heterogeneity of the peroxidase enzymes isolated from human neutrophils. In this study, fast protein liquid chromat...