Abstract
A method is presented for deriving a highly purified acid protease from calf thyroid. Thyroglobulin hydrolysis was very slow at pH 3.5 in comparison to hemoglobin hydrolysis. Protease was purified 285-fold from thyroid supernatant fraction by DEAE+Cellulose and Sephadex G-200 chromatography. The protein sedimented as a single component in the analytical centrifuge with a sedimentation constant of 3.6 S. Enzyme activity of the purified enzyme was increased by mercaptoethanol and cyste ne, and inhibited by n-chloromercuribenzoate.A specific antibody against purifisd human-acid protease was produced in rabbits.In the sera of patients with various thyroid diseases, antibody titers against acid protease were examined. No positive antibody titer was observed. The relation between the auto-immune disease in thyroid and antibody formation to acid protease is discussed.
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