title: Enhanced stability of erythrocyte-entrapped glucocerebrosidase activity.
abstract: The stability of free glucocerebrosidase activity has been compared with the stability of glucocerebrosidase entrapped in hemolyzed, resealed erythrocytes. Encapsulation markedly stabilizes the enzyme, partly by providing an environment with a high protein concentration. In addition, in the presence of glucose, enzyme activity and GSH content remain constant, but in its absence, enzyme activity and GSH levels fall, indicating the existance of an additional, metabolically linked protective mechanism. Since the free enzyme is inactivated by p-CMB and is protected by DTT, it is likely that GSH generated by the pentose phosphate pathway protects essential sulfhydryl groups of glucocerebrosidase.
mesh_terms: D002352:Carrier Proteins / Q000378:metabolism; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D004912:Erythrocytes / Q000201:enzymology*; D005260:Female; D005947:Glucose; D005959:Glucosidases / Q000378:metabolism*; D005962:Glucosylceramidase / Q000378:metabolism*; D006207:Half-Life; D006801:Humans; D009249:NADP / Q000494:pharmacology; D011247:Pregnancy; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013696:Temperature
chemical_list: D002352:Carrier Proteins; D002729:Chloromercuribenzoates; D012710:Serum Albumin, Bovine; D009249:NADP; D005959:Glucosidases; D005962:Glucosylceramidase; D005947:Glucose; D004229:Dithiothreitol