Microbeam X-ray spectrometry, energy-dispersive X-ray fluorescence ana
lysis, and neutron activation analysis were evaluated for the detectio
n of selenium contained in the selenoprotein glutathione peroxidase. T
he glutathione peroxidase had been previously separated using polyacry
lamide gel electrophoresis. The use of Bragg-reflected polarized X-ray
beams was employed in the X-ray fluorescence measurements to minimize
the problem of scatter owing to the gel matrix. Current detection lim
its of selenium in a gel matrix are 2.1 ng in the bench-top microbeam
X-ray system and 30-60 ng using XRF with polarized beams. Neutron acti
vation analysis was used for quality-control measurements, with a dete
ction limit here of < 0.08 ng. The work has in principle established t
he feasibility of such an approach.