¹ From the Department of Chemistry, The City College of the College of the City of New York

1. Acid-inactivated yeast invertase could not be regenerated in the presence of the proteolytic enzymes trypsin, pepsin, and chymotrypsin.

2. Certain foreign proteins of non-enzymatic nature partially inhibited the reactivation of acid-inactivated invertase.

3. Certain proteins as gelatin, lacto-globulin, and carbohydrate-free horse crystalbumin did not prevent the reactivation of invertase at all.

4. Highly purified reactivated invertase was shown to exhibit an effect typical of original native invertase; that is, acceleration of its activity in presence of foreign protein at pH 3.0.

5. Native invertase was not digested by trypsin and chymotrypsin.

6. The addition of trypsin and chymotrypsin to reactivating invertase did not affect the invertase which had already reverted to the active form, but prevented further reactivation of inactive invertase.

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