Transport of organic compounds in the mammal. Partition of dieldrin and telodrin between the cellular components and soluble proteins of blood

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Abstract
In "chrbmatographic" experiments, Telodrin interacts with sodium taurocholate and with bovine albumin, not with gelatin. Solubilities of dieldrin and Telodrin are 4000 times as great in rabbit serum as in water. Dieldrin and Telodrin are located mainly in the erythrocyte contents and plasma of rabbit and rat blood and not in the leucocytes, platelets or stroma. On electrophoretic evidence at pH 8.6, dieldrin and Telodrin are associated with hemoglobin and an unknown constituent in the erythrocyte contents, with albumin and [alpha]-globulin in rabbit serum, and with pre- and post-albumin in rat serum. In rabbit and rat serum at pH 4.5, these substances are partially separated into 4 zones by electrophoresis. Ultracentri-fugation of rabbit serum causes flotation of a proportion of Telodrin with high-density lipoprotein which has similar electrophoretic properties to those of [alpha]1-globulin. DEAE-cellulose-column chromatog-raphy separates from rabbit serum three bands of radioactive dieldrin or Telodrin, associated with albumin, the a-globulins and a protein with the same electrophoretic mobility as albumin respectively. After intraperitoneal injection of single doses of [C14] dieldrin or [C14] Telodrin into the rat, the radioactivity in blood is shared between plasma and cells, and the ratio remains roughly constant for 4 days. The very rapid initial rate of removal of dieldrin or Telodrin from blood is followed by a rougly logarithmic rate of removal. Dieldrin and Telodrin do not interfere with the binding of 3,3[image],5-tri [I131] iodothyronine to serum proteins. Free permeability of the erythrocyte surface to the insecticides is suggested by the proportionation of dieldrin and Telodrin between blood plasma and cells in vivo at different times and different concentrations.