A soluble extract of neutrophil granules interfered with activation of the NADPH oxidase in a cell-free system. The extract had no effect on superoxide production by preactivated enzyme. The inhibitory activity was retained during dialysis and was lost upon exposure to proteinase K indicating that the active substance was a protein. The inhibitor exhibited a high stability at elevated temperatures. Chromatography of granules extract on ion exchangers implied that the inhibitor was a positively charged protein eluting from S Sepharose cation exchanger above 0.4M concentration of NaCl.
|Number of pages||5|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - 31 May 1990|