Abstract
The wall-bound invertase of morning-glory callus was solubilized by a systematic treatment with several chemicals. The degree of solubilization of wall-bound invertase was drastically altered by varying the pH values and chemical composition of the buffers. Triton X-100 and sucrose did not release invertase from cell walls. Comparative studies were made of some properties of wall-bound and solubilized invertases. These results suggest that the linkage of the enzyme to the cell wall is ionic. The cytoplasmic acid invertase, like the enzyme solubilized from cell walls, was adsorbed on cell walls, but the cytoplasmic neutral invertase was not. Based on these results, the linkage of acid invertase to cell walls, and a possible interrelationship and physiological role of both acid invertases and neutral invertase were discussed.
