Dextran enzyme inhibitors, effect

The hydrolysis of maltose by glucoamylase has been studied in the absence and presence of dextran and dextran sulphate. Dextran became bound to glucoamylase and was a non-competitive inhibitor of the enzyme. The reaction rate was hardly affected at pH 4.0-4.5 by dextran sulphate addition but depended considerably on dextran sulphate at pH 3.5, suggesting some kind of interaction between the two. The transport and metabolism of dextran [ S] sulphates of various molecular weights and sulphur contents in rat intestinal mucosa, and the effects of calcium thereon, have been investigated. Results suggested that dextran sulphates are transferred by pinocytosis and other mechanisms and are then desulphated mainly in microsomes, and subsequently become depolymerized. 

---