Large-scale purification of myeloperoxidase from HL60 promyelocytic cells: characterization and comparison to human neutrophil myeloperoxidase
HR Hope, EE Remsen, C Lewis Jr… - Protein expression and …, 2000 - Elsevier
A large-scale purification procedure was developed for the isolation of myeloperoxidase
from HL60 promyelocytic cells in culture. Initial studies showed the bulk of peroxidase-
positive myeloperoxidase activity to be located in the cetyltrimethylammonium bromide
solubilized particulate fraction of cell homogenates. The myeloperoxidase was then
chromatographically purified using concanavalin A followed by gel filtration. SDS–PAGE
analysis of the final preparation showed the presence of only two proteins with molecular …
from HL60 promyelocytic cells in culture. Initial studies showed the bulk of peroxidase-
positive myeloperoxidase activity to be located in the cetyltrimethylammonium bromide
solubilized particulate fraction of cell homogenates. The myeloperoxidase was then
chromatographically purified using concanavalin A followed by gel filtration. SDS–PAGE
analysis of the final preparation showed the presence of only two proteins with molecular …
