Abstract
Previous observations have suggested that lipoproteins may be involved in the transport of selenium in humans. To further investigate this question, selenium was measured in lipoprotein fractions isolated from plasma of healthy adults. A gas chromatographic–mass spectrometric method using the isotopic dilution technique was developed to ensure a reliable measurement of low amounts of selenium. About 3% of total plasma selenium was bound to lipoproteins, mainly to the LDL fraction. After solvent fractionation of LDL and HDL, the major part of the selenium was recovered in the protein extract, suggesting 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 participating in a selenium–sulphur bond. This could explain why the amount of selenium bound to apolipoprotein B in LDL was about twice that which could be expected from a random substitution of selenomethionine for methionine.
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