Abstract
Aluminium is known to cross the blood brain barrier and gain entry to the CNS via the endogenous iron transport protein transferrin. The extent to which Al-Tfn binding and Al-Tfn intra-cellular movement corresponds to that of Fe-Tfn is unknown. Characterising these processes may help us to understand the mechanics underlying Al transport and therefore its role in neurodegenerative disorders such as Alzheimer’s and dialysis dementia. pH binding was studied using fractions eluted via biorad size exclusion chromatography columns at pH 5.0 and 6.8 and using a buffer/mobile phase of 100mM malic acid solution. The fraction yields were analysed using Unicam PYE atomic absorption spectroscopy apparatus, P9000 furnace. All liver microsomal samples showed significant interference to a degree where greater than 90% of the aluminium present remained undetected. This interference effect was reproduced with the simple matrices KCl and sucrose but not with malic acid. The analysis of aluminium content of the SEC fractions from Al-Tfn samples at pH 5.0 and 6.8 showed no differences in elution profile- and an early elution of aluminium within a fraction volume incompatible with the molecular weights of either transferrin or free aluminium. The results from both GFAAS and SEC indicated that the experimental techniques were unsuitable for achieving the objectives. This conflicts with previous work. Further experiments to isolate or minimise the source of the GFAAS interference and SEC early elution are recommended.