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Physical and kinetic properties of β‐glucosidase in Gaucher disease
Author(s) -
Karazeh A.,
Carroll M.
Publication year - 1983
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf01800734
Subject(s) - enzyme , concanavalin a , biochemistry , enzyme replacement therapy , chemistry , ammonium , solubilization , spleen , disease , medicine , organic chemistry , in vitro
Membrane‐bound ‘acid’ β‐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 β‐glucosidase was activated by taurocholate, whereas the Gaucher enzyme was inhibited. The decrease in ‘acid’ β‐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’ β‐glucosidase in type 1 Gaucher disease.