1969 Volume 65 Issue 4 Pages 545-552
Rabbit intestinal sucrase, which is associated with the microvillous membrane of the mucosal cell, was solubilized with papain [EC 3. 4. 4. 10] and purified by utilizing its reversible adsorption on Sephadex G-200 and gel filtration on Bio-Gel P-300.
The purified enzyme was homogeneous on ultracentrifugation and disc electrophoresis analyses. The sedimentation coefficient (s020, W) of the enzyme was 10.OS and its molec-ular weight was estimated to be approximately 235, 000 by the Archibald method.
It hydrolyzed maltose and α-methylglucoside in addition to sucrose, but not α, α-trehalose. β-Glucosides and α- and β-galactosides tested were not hydrolyzed. Melezi-tose served as a substrate but raffinose did not. Furthermore, the maltase activity present in the homogenate paralleled to the sucrase activity during purification. These findings indicate that the enzyme is a glucosido-sucrase or an a-glucosidase [EC 3. 2. 1. 20].
Other enzymatic properties such as pH optimum, Michaelis constant, activators and inhibitors were studied.