Abstract
A procedure for the iodination of lipid A is described. The iodinated product binds to rabbit spleen cells but not to red blood cells, and the binding to such spleen cells is inhibited by the presence of an excess of unlabeled lipid A. In dilute buffer solution, 125I-labeled lipid A appears to be aggregated because it migrates on Sephadex G-100 in the region of the void volume, whereas it migrates as would a molecule even smaller than cytochrome c upon electrophoresis on polyacrylamide gel in the presence of sodium dodecyl sulfate. Evidence is presented that is consistent with the view that the iodine label is associated with the O-acyl groups of lipid A.
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