Physical and kinetic properties of beta-glucosidase in Gaucher disease.
Membrane-bound 'acid' beta-glucosidase of human spleen was solubilized with either sodium cholate or 'Cutscum'. The solubilized enzyme in type 1 (adult) Gaucher disease was less heat-stable than the normal enzyme, and when precipitated by ammonium sulphate it had a higher apparent molecular weight than the corresponding normal enzyme. The normal beta-glucosidase was activated by taurocholate, whereas the Gaucher enzyme was inhibited. The decrease in 'acid' beta-glucosidase activity in Gaucher disease was associated with a profound deficiency of that form of the enzyme which bound to Concanavalin A. The results are consistent with faulty processing of newly synthesized 'acid' beta-glucosidase in type 1 Gaucher disease.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003208:Concanavalin A / Q000378:metabolism; D005776:Gaucher Disease / Q000201:enzymology*; D005959:Glucosidases / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D012995:Solubility; D013154:Spleen / Q000201:enzymology; D013656:Taurocholic Acid / Q000378:metabolism; D001617:beta-Glucosidase / Q000378:metabolism*
D003208:Concanavalin A; D013656:Taurocholic Acid; D005959:Glucosidases; D001617:beta-Glucosidase