Abstract
The enzyme guanine deaminase was found in lingcod muscle and a study of its properties carried out. In the crude state, two pH optima were found, one of which was lost on purification. Of several guanine analogues tested, only 8-azaguanine was deaminated by the enzyme. A number of compounds were tested as inhibitors. No cofactors were required. A purification of over 200-fold is described which involves three steps. The Km was determined as 3.3 × 10−5 M.
Publisher
Canadian Science Publishing
Cited by
10 articles.
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