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Journal Of Toxicology And Environmental Health • August 1996<br />

Speciation of aluminum in biological systems<br />

Author information<br />

Harris WR1, Berthon G, Day JP, Exley C,<br />

Flaten TP, Forbes WF, Kiss T, Orvig C, Zatta PF.<br />

Department of Chemistry<br />

University of Missouri-St. Louis 63121 USA<br />

Abstract<br />

As a “hard”, trivalent metal ion, Al3- binds strongly to oxygen-donor ligands such as<br />

citrate and phosphate. The aqueous coordination chemistry of Al is complicated by<br />

the tendency of many Al complexes to hydrolyze and form polynuclear species, many<br />

of which are sparingly soluble. Thus there is considerable variation among the Al<br />

stability constants reported for several important ligands. The complexity in the aqueous<br />

chemistry of Al has also affected Al toxicity studies, which have often utilized<br />

poorly characterized Al stock solutions. Serum fractionation studies show that most<br />

Al is protein bound, primarily to the serum iron transport protein transferrin. Albumin<br />

appears to play little, if any, role in serum transport. There is little agreement as to<br />

the speciation of the remaining low-molecular mass fraction of serum Al. The lability<br />

of the Al3+ion precludes the simple separation and identification of individual Al<br />

complexes. Computational methods are available for detailed computer calculations<br />

of the Al speciation in serum, but efforts in this area have been severely hampered<br />

by the uncertainties regarding the stability constants of the low molecular mass Al<br />

complexes with citrate, phosphate, and hydroxide. Specific recommendations for<br />

further research on Al speciation include: (1) Determine more accurate Al stability<br />

constants with critical low molecular mass ligands such as citrate and phosphate; (2)<br />

supplement traditional potentiometric studies on Al complexes with data from other<br />

techniques such as 27Al-NMR and accelerator mass spectrometry with 26Al; (3)<br />

develop new methods for generating reliable linear free energy relationships for Al<br />

complexation; (4) determine equilibrium and rate constants for Al binding to transferrin<br />

at 37 degrees C; (5) confirm the possible formation of low-molecular-mass Alprotein<br />

complexes following desferrioxamine therapy; (6) continue research efforts<br />

to incorporate kinetic considerations into the present equilibrium speciation calculations;<br />

(7) improve methods for preparing chemically well-defined stock solutions for<br />

toxicological studies; (8) incorporate more detailed speciation data into studies on Al<br />

toxicity and pharmacokinetics; and (9) incorporate more detailed speciation data into<br />

future epidemiological studies on the relationship between Al toxicity and various<br />

water quality parameters.<br />

[this report explains why determining the fate<br />

of aluminum in the human body is so difficult]<br />

http://www.ncbi.nlm.nih.gov/pubmed/?term=8772798

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