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A partially purified fraction of human thyroid-stimulating hormone (DEAE-II) was further purified by ion-exchange chromatography on IRC-50, gel-filtration on Sephadex G-100 and finally chromatography on DEAE-cellulose. Two fractions were obtained which were high in thyroid-stimulating activity (8·3 and 7·3 units human Research Standard A/mg) and were comparable in potency to other preparations of the human hormone reported in the literature. They were also electrophoretically heterogeneous as were the preparations of other workers. Lipolytic activity toward cells obtained from human or rat adipose tissue was demonstrated for all fractions containing thyroid-stimulating activity, the two activities being roughly parallel. It is concluded that both thyroid-stimulating and lipolytic activities are probably present in the same protein molecule, but it is unlikely that the latter activity is of physiological significance.