Hydrodynamic Properties of the Sucrase Isomaltase Complex from Rabbit Small Intestine

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Abstract
From the hydrodynamic properties of the sucrase · isomaltase complex at low ionic strength, a molecular weight of 221000 was calculated. The complex dimerizes at high ionic strength. Under denaturing conditions the complex dissociates into two subunits of identical or almost identical molecular weight (112000) which are presumably composed of one polypeptide chain each. The isomaltase subunit, isolated in enzymatically active form, has a molecular weight of 113000.