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Isolation of glycine from hydrolyzates of the plasma proteins obtained at 4 hours after injection and deter­ mination of its radioactivity showed an increase in the S.A. of glycine of the vitamin E-deficient group pro­ portional to the increase observed with the proteins. It may therefore be assumed that the higher protein S.A. is caused by a higher rate of glycine-14C incor­ poration. The effect of vitamin E-deficiency on the in­ corporation rate of labeled glycine is thus not limited to the proteins of skeletal m uscle6. As O p p e n h e im e r et al. 2 have shown that the protein nitrogen content of plasma is unaffected by the deficiency disease, an increased rate of plasma protein synthesis should be accompanied by an equal increase in the rate of plasma protein catabolism. The higher incorporation rate observed with the vit­ amin E-deficient animals is not caused by a higher S.A. of the unbound serum glycine, as there is no significant difference between the S.A. of free serum glycine in vitamin E deficient and control rabbits 3. The possibility that the S.A. of the free glycine pool in liver might be higher in the deficient animals is under investigation. Since the serum proteins, with the exception of the gamma-globulin fraction, are synthesized in the liver, the results here presented indicate that vitamin E-defi­ ciency in the rabbit has a pronounced effect on the functioning of the liver.

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