Abstract
The addition of a suspension of erythrocytes from rabbit, pig, ox, rat or human to vitamin A alcohol, dissolved in ethanol, results in rapid lysis of the cells and production of erythrocyte stroma on incubation at 37[degree]. Homologous serum inhibits lysis. Erythrocytes suspended in a medium containing sucrose and NaCl are more easily lysed than those in NaCl solution alone. The temperature-dependence of the release of hemoglobin by vitamin A is similar to that of the release of protease from rat-liver lysosomes treated with the vitamin. Hemolysis produced by vitamin A has been compared with that caused by a neutral detergent and by lysolecithin. Only weak hemolytic activity is possessed by hydrogenated vitamin A, oxidized vitamin A, anhydro-vitamin A, vitamin A2 alcohol and vitamin A2 aldehyde. B-Ionone, geraniol, citral, phytol and dodecanol are without activity at the concentrations tested. Changes in the nature of the end group or the chain length of the molecule result in diminished hemolytic activity. The molecular specificity for lysis is similar to that for biological activity and for action on isolated lysosomes. The hypothesis is presented that the site of action of the vitamin is at the lipoprotein membranes of cells and their organelles and that is function is the control of the permeability of biological membranes.

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