Abstract
1. 1. Both acid and neutral α-glucosidases are characterized in 4 human adenocarcinoma tumors obtained from SW-480, HCT-8R, HRT-18, HT-29 cell-lines of different glycogen content, by using either 4-methyl-umbelliferyl-α- d-glucoside (MUαG) or glycogen and maltose as substrate. 2. 2. No obvious linear relationship between glucosidases activity and glycogen level can be found; however, the lowest and highest activities coincide with the lowest and highest glycogen contents respectively. 3. 3. The hydrolytic activity of neutral glucosidase investigated in the presence of turanose as inhibitor of the acid form, is found to be high towards MUαD or maltose, but weak towards glycogen. 4. 4. Kinetic parameters for both enzymes are found to be similar in the 4 tumors under investigation and close to what was reported in normal animal tissues.
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