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Marked increase of methylumbelliferyl‐tetra‐ N ‐acetylchitotetraoside hydrolase activity in plasma from gaucher disease patients
Author(s) -
Tandt W. R.,
Hoof F.
Publication year - 1996
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/bf01799265
Subject(s) - enzyme replacement therapy , enzyme , substrate reduction therapy , enzyme assay , hydrolase , krabbe disease , lysosomal storage disease , endocrinology , medicine , disease , gaucher's disease , fabry disease , activator (genetics) , glucocerebrosidase , alpha galactosidase , plasma levels , specific activity , chemistry , biochemistry , receptor , leukodystrophy
Summary Methylumbelliferyl‐tetra‐ N ‐acetylchitotetraoside hydrolase activity was increased 53‐ to 484‐fold in plasma from Gaucher disease patients and no activator could be found. High activity was also measured in other lysosomal storage diseases including Krabbe disease, Wolman disease, GM 1 ‐gangliosidosis and to a lesser extent Niemann‐Pick disease type B, but the activities were lower than the lowest values in Gaucher patients. Kinetic properties of the high activity in Gaucher plasma were similar to those of controls. It is not known whether the increased activity represents intrinsic enzyme activity or increased enzyme concentration. It is possible that this enzyme may help in the detection of Gaucher disease or in the assessment of enzyme therapy with β ‐ d ‐glucosidase (Ceredase®).