PURIFICATION OF THYROID PROTEASES BY CELLULOSE COLUMN CHROMATOGRAPHY

Abstract
Several methods for purification of thyroid protease have been investigated. Chromatography on diethylaminoethyl and carboxymethyl cellulose resulted in purification and separation of two distinct acidic proteases. One protease shewed a pH optimum of 3.8 and the other 5.7. A combination of chromatography on both types of cellulose columns resulted in 500 fold purification of both enzymes.