Abstract
The enzymatic activity of guinea pig myeloperoxidase (MPO) and eosinophil peroxidase (EP) was compared on the following substrates: guaiacol, aspartic acid and histamine. EP manifested a 4 fold activity per cell compared with MPO in peroxidation of guaiacol. The ability of PMN to degrade aspartic acid by peroxidative deamination was confirmed and the ability to degrade histamine established. Eosinophils, however, showed no activity on both substrates despite their known antihistaminic properties.
| Original language | English |
|---|---|
| Pages (from-to) | 141-145 |
| Number of pages | 5 |
| Journal | RES Journal of the Reticuloendothelial Society |
| Volume | 17 |
| Issue number | 3 |
| State | Published - 1975 |
