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ENZYMOLOGICAL DIAGNOSIS OF A GROUP OF LYSOSOMAL STORAGE DISEASES: REVIEW OF 5‐YEAR EXPERIENCE OF 1600 PATIENT‐SAMPLE REFERRALS
Author(s) -
Pollard Anthony C.,
Carey William F.,
Nelson Paul V.,
Poulos Alfred,
Hill Geoffrey N.
Publication year - 1980
Publication title -
medical journal of australia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 131
eISSN - 1326-5377
pISSN - 0025-729X
DOI - 10.5694/j.1326-5377.1980.tb100764.x
Subject(s) - sandhoff disease , gangliosidosis , metachromatic leukodystrophy , lysosomal storage disease , mucolipidosis , fabry disease , krabbe disease , hexosaminidase , niemann–pick disease , disease , enzyme replacement therapy , enzyme , tay sachs disease , arylsulfatase a , medicine , alpha galactosidase , hexa , pathology , biology , biochemistry , leukodystrophy
Lysosomal acid hydrolase activities have been measured in extracts of peripheral blood leucocytes of approximately 1600 patients referred from throughout Australia, each of whom was suspected of having a neurolipidosis. Assays for 12 different lysosomal enzymes were performed on each patient as a routine; ten assay systems were based on commercially available substrates, and four used radiolabeled glycosphingolipids prepared in our own laboratory. Of the 85 patients with positive results, 81 were diagnosed as being homozygous‐deficient for a particular lysosomal enzyme. These patients comprised nine with GM 1 ‐gangliosidosis, 12 with GM 2 ‐gangliosidosis (11 of Tay‐Sachs' disease and one of Sandhoff's disease), 18 with trihexosylceramide lipidosis (Fabry's disease), eight with β‐galactosylceramide lipidosis (Krabbe's disease), 14 with β‐glucosylceramide lipidosis (Gaucher's disease), two with sphingomyelin lipidosis (Niemann‐Pickdisease), 13 with metachromatic leucodystrophy and five with á‐mannosidosis. In addition, four patients were diagnosed as being affected with mucolipidosis Type II (I‐cell disease), based on elevated plasma lysosomal enzyme activities, making a total of 85 homozygous‐affected patients. Clinically the patients showed wide phenotypic variability within each of the enzyme‐deficient states, which did not appear to correlate with the level of “residual” enzyme activity in their leucocyte extracts.