Search

The visualization, by confocal Raman microscopy, of the intracellular distribution of two enzymes important in the immune eosinophil peroxidase (EPO) in eosinophils is reported. The effect of photobleaching of the Raman signal at 413.1 nm excitation on the reconstructed Raman images is discussed.

Hypophalous acids (HOX), which are produced by activated neutrophils, monocytes, eosinophils and possibly macrophages are crucial for immune response. However, excessive or misplaced generation can damage host tissues.

The Charcot-Leyden crystal (CLC) protein has been one of the most interesting subjects of biochemistry research due to its undetermined link with eosinophil functions. Diffraction data derived from a sample of CLC cyrstals, however, suggest that these proteins do not actually have affinity for beta-galactosides. Results further indicate that CLC proteins bind with mannose in a manner distinct with other galectin compounds.

A novel fluorescent chemosensor is developed that has used the [Zn.sup.2}-DPA (DPA = dipicolylamine) complex, which has selectively targeted flavin adenine dinucleotide (FAD) from among other flavins in water. This detector is used to detect the FAD in eosinophils by fluorescence microscopy and fluorescence-activated cell sorter (FACS).

A study was conducted to analyze the function of eosinophil peroxidase and myeloperoxidase in supporting protein oxidative damage through bromination. The role of protein tyrosine residues as endogenous traps of reactive brominating species promoting stable ring-brominated adducts was examined. Results indicated that 3-bromotyrosine and 3,5-dibromotyrosine can function as molecular markers for oxidative damage of proteins through reactive brominating species in vivo.