ENHANCED STABILITY OF ERYTHROCYTE-ENTRAPPED GLUCOCEREBROSIDASE ACTIVITY

  • 1 January 1980
    • journal article
    • research article
    • Vol. 96  (4) , 682-692
Abstract
The stability of free glucocerebrosidase activity was compared with the stability of glucocerebrosidase entrapped in hemolyzed, resealed [human] erythrocytes. Encapsulation markedly stabilizes the enzyme, partly by providing an environment with a high protein concentration. In the presence of glucose, enzyme activity and GSH [glutathione] content remain constant, but in its absence, enzyme activity and GSH levels fall, indicating the existence of an additional, metabolically linked protective mechanism. Since the free enzyme is inactivated by p-CMB [p-chloromercuribenzoate] and is protected by DTT [dithiothreitol], it is likely that GSH generated by the pentose phosphate pathway protects essential SH groups of glucocerebrosidase. [Applicability of this study to enzyme replacement therapy in Gaucher''s disease is discussed].