Comparative metal content profiling of parasitic helminths by electron paramagnetic resonance spectrometry: significance for metalloprotein content.
Variation in co-ordination geometries of metal ions bound to proteins imposes electronic states different from free (hydrated) ions in solution. Electron paramagnetic resonance spectroscopy has been used to analyse a selection of parasitic helminths for metal content as an initial step to determination of metallo-enzymes in their ES products under immune stress conditions. Characteristic paramagnetic resonance spectroscopy spectra show clear evidence for the presence of iron, copper, and manganese centres and in the selected parasites. The metals ions are identified as protein-bound as distinct from free metal ions present in aqueous solution, and distinguishable from parasite dietary components derived from host sources. Indication is given that superoxide dismutases may, in part, account for the metal ions observed. The use of electron paramagnetic resonance spectroscopy to identify specific protein-bound metals without prior isolation of the suspected protein is here applied.
Taiwo
F A
FA
School of Pharmacy and Pharmaceutical Sciences, De Montfort University, Leicester, UK. ttaiwo@dmu.ac.uk
Brophy
P M
PM
Pritchard
D I
DI
Brown
A
A
Wardlaw
A
A
Patterson
L H
LH
D000818:Animals; D004578:Electron Spin Resonance Spectroscopy; D006376:Helminths / Q000737:chemistry*; D008667:Metalloproteins / Q000032:analysis*; D019216:Metals, Heavy / Q000032:analysis*
D008667:Metalloproteins; D019216:Metals, Heavy