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Abstract
The plasma membrane-bound NADPH-cytochrome c reductase of guinea pig macrophages (Mφ) was found to be phosphorylated when [ 32P]phosphate-labeled cells were stimulated with 12-phorbol 13-myristate acetate (PMA). The time course of phosphorylation was parallel to that of O − 2-generating activity elicited. These results suggest that the reductase participates as a flavoprotein in activation of the respiratory burst NADPH oxidase, when phosphorylated.
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