Abstract
The enzyme guanine deaminase was found in lingcod muscle and a study of its properties carried out. In the crude state, 2 pH optima were found, 1 of which was lost on purification. Of several guanine analogues tested, only 8-azaquanine 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 3 steps. The Km was determined as 3.3 X 10-5 M.

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