Isolation of thyroidal acid protease and immunological analysis of its antibody.

نویسندگان

  • Y Ochi
  • L J Degroot
چکیده

hydrolysis. Protease was purified 285-fold from thyroid supernatant fraction by DEAWCellulose 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 cysteine, 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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عنوان ژورنال:
  • Endocrinologia japonica

دوره 17 6  شماره 

صفحات  -

تاریخ انتشار 1971