Interaction of Mercurials with Salmon Serum Lipoproteins

Details Interaction of Mercurials with Salmon Serum Lipoproteins Interaction of Mercurials with Salmon Serum Lipoproteins

Feb 1974

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1974natur.247..569r&link_type=abstract

Nature, Volume 247, Issue 5442, pp. 569-570 (1974).

Physics

Scientific paper

ALTHOUGH the toxic effects of mercury and its derivatives are well known1-7 relatively little is known about the transport mechanisms involved in its distribution throughout the body. One possible means could be the serum lipoproteins through reactions involving lipids and proteins. Various metal ions bind with phospholipids8; for example, calcium ions bind to anionic sites of phospholipids in lipid monolayers9. In addition, phospholipids provide negatively charged sites for calcium ion exchanges in biomembranes10 and contribute to the transport of ferrous ions in biphasic systems11. These findings, together with the fact that mercurials bind with negative sites of proteins, led us to explore the possibility that mercurials are actively sequestered by the serum lipoproteins.

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