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The exophthalmogenic activity of the beta subunit of bovine thyrotropin is only 10% to 20% that of the thyrotropin molecule or of an exophthalmogenic factor produced by partial pepsin digestion of purified thyrotropin preparations. The alpha subunit of thyrotropin, luteinizing hormone, and both subunits of luteinizing hormone have no exophthalmogenic activity.

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The present report demonstrates that mouse tumor thyrotropin preprarations have exophthalmogenic activity. In addition it shows that the exophthalmogenic activity of mouse tumor thyrotropin can be increased by partial pepsin digestion, whereas the thyroid stimulating activity of mouse tumor thyrotropin is rapidly destroyed by such treatment. Thus, after 30 min of pepsin digestion, mouse tumor thyrotropin has 130% of its initial exophthalmogenic action but only 10% of its thyroid stimulating activity.

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