Previous observations have suggested that lipoproteins may be involved in t
he transport of selenium in humans. To further investigate this question, s
elenium was measured in lipoprotein fractions isolated from plasma of healt
hy adults. A gas chromatographic-mass spectrometric method using the isotop
ic dilution technique was developed to ensure a reliable measurement of low
amounts of selenium. About 3% of total plasma selenium was bound to lipopr
oteins, mainly to the LDL fraction. After solvent fractionation of LDL and
HDL, the major part of the selenium was recovered in the protein extract, s
uggesting that it may be incorporated in apolipoproteins. The exact form of
Se is not yet clearly established. Considering the different Se compounds
found in proteins, it is postulated to be selenomethionine, and/or particip
ating in a selenium-sulphur bond. This could explain why the amount of sele
nium bound to apolipoprotein B in LDL was about twice that which could be e
xpected from a random substitution of selenomethionine for methionine. (C)
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