Abstract
Certain properties of insoluble yeast invertase, i.e., invertase more or less in the native state, anchored in or on insoluble structures of the yeast cell, have been compared to the corresponding properties of the enzyme in true solution. It has been found that groups in the invertase molecule whose existence in the dissolved enzyme has been proven by experiments on the influence of H + ions and inhibitors must be assumed to occur in the native, insoluble enzyme in such positions on the particle surface that they are freely accessible to substances in the surrounding medium. The nature of certain groups essential for the enzymic activity has been discussed.
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