Uptake of antimony potassium tartrate by mouse liver slices.

1. The uptake of (124)Sb-antimony potassium tartrate by isolated mouse liver slices has been measured and found to establish high tissue: medium concentration ratios.2. Uptake was not influenced by oxygen lack, potassium, ouabain, dinitrophenol or sodium arsenate. It was inhibited by dimercaprol and reduced at low temperature. No evidence was found of counter-transport. After subcellular fractionation, most of the radioactivity was recovered from particulate fractions.3. Kinetic studies of uptake from media containing different concentrations of antimony suggest that uptake is due partly to diffusion and partly to a saturable binding mechanism, probably involving chelation by non-diffusible thiol groups. Saturation studies suggest that only a small proportion of thiol groups bind antimony, the remainder undergoing catalytic oxidation.