RT Journal
A1 Daniels LB, Coyle PJ, Glew RH, Radin NS, Labow RS
T1 BRain glucocerebrosidase in gaucher's disease
JF Archives of Neurology
JO Archives of Neurology
YR 1982
FD September 1
VO 39
IS 9
SP 550
OP 556
DO 10.1001/archneur.1982.00510210020005
UL http://dx.doi.org/10.1001/archneur.1982.00510210020005
AB • Using glucocerebroside labeled with carbon 14 as the substrate, we determined that homogenates of brain tissue from both neuropathic and nonneuropathic cases of Gaucher's disease were profoundly deficient (more than 85%) in glucocerebrosidase activity. The β-glucosidase activity, as measured with 4-methylumbelliferyl-β-D-glucopyranoside as the substrate, in the homogenates of brain from four cases of Gaucher's disease was less sensitive to inhibition by conduritol B epoxide (CBE) when compared with normal brain β-glucosidase. However, when homogenates were assayed with radiolabeled glucocerebroside as the substrate, no differential sensitivity toward CBE was indicated, suggesting the presence of an additional, CBE-insensitive, β-glucosidase in brain tissue. Residual glucocerebrosidase activity partially purified from the brain of an adult with type 1 Gaucher's disease was activated threefold by gluconoyl hydrazine, whereas the same enzyme from control brain was unaffected, and eight times less sensitive to gluconolactone inhibition.