The fact that isolated cell nuclei are capable of metabolizing carbohydrate at least to the stage of pyruvate or of ribose formation (1, 2) may be taken to mean that in the course of their intracellular metabolism nuclei will reduce either the glycolytic coenzyme DPN, or the hexosemonophosphate dehydrogenase coermyme TPN. The intensity of such metabolism being similar in nucleus and cytoplasm, the proportion of total cell coenzyme reduced by the nucleus will vary with its size---some 10 per cent in a liver cell, about 50 per cent in a thymus cell. Since the coenzymes in question are not terminal acceptors of hydrogen but serve only to mediate its transfer, it is a requirement of nuclear metabolism that mechanisms exist whereby reduced nuclear coenzylnes become reoxidized. Little, however, is known about the possibilities of hydrogen transfer in nuclei, and the present communication is therefore addressed to this problem.It is almost certain that nuclei cannot transfer hydrogen to molecular oxygen, a relation unequivocally demonstrated for cytochrome oxidase in rat liver by Hogeboom, Schneider, and Striebich (3). Thus, the ultimate problem of nuclear coenzyme reoxidation--at least for aerobic cells--resolves itself into a search for pathways of hydrogen transfer between nucleus and cytoplasm. No better situation illustrative of this point is to be found than in calf thymus where the nucleus accounts for 60 per cent of total cell mass. Although the nuclei of this tissue are capable of accounting for half the glucose-6-phosphate metabolized (2), it is clear from the data of Table II that the capacity to react with molecular oxygen is entirely restricted to the particles of the peripheral cytoplasm.The restriction of terminal oxidation to autonomous mitochondrial bodies means in effect that the reoxidation of coenzymes, reduced in the course of intermediary carbohydrate metabolism, is a problem common to cytoplasm and nucleus. It will be seen, however, that cytoplasm and nucleus do not share the same mechanisms in response to this common need, even though it is ira-* Present address: