CATECHOLASE (TYROSINASE) :* REVERSIBLE INACTIVATION AND REACTIVATIONt
نویسنده
چکیده
Studies of the chemical properties of the enzyme, catecholase, have shown that this polyphenoloxidase consists of a copper-protein complex (l-3). Indications have also been obtained that the enzymic activity of catecholase is associated with the copper part of the molecule, since it has been found that the addition of certain reagents known to react with cupric ions will inhibit the enzymic activity of catecholase preparations (1, 2, 4, 5). We were interested to find out whether the enzyme, so inactivated, could be reactivated by the addition of certain metal ions. Cupric, ferric, cobaltous, and manganous ions were tested. In the following we wish to report on our findings.
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