Abstract
In this paper, an adsorption procedure of urease to Al(OH) 3 is described that leads to a water-insoluble catalyst for urea hydrolysis. Moreover, it can be shown by this example, that the quantitative interpretation of adsorption measurements provides an indirect method for obtaining information about the structure of the adsorbed enzyme. The results of the experiments reported here reveal that, within two concentration ranges, the adsorbed quantity of enzyme increases with different slopes. This kind of adsorption is explained by a model, the basis of which is the assumption of a structure for the enzyme molecule deviating from the spherical form. The measured activities of the assays, as a function of adsorbed enzyme, support the hypothesis propounded.
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