Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 198-202 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 169 |
| Issue number | 1 |
| DOIs | |
| State | Published - 31 May 1990 |