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Mucolipidosis II and III: different residual activity of beta‐galactosidase in cultured fibroblasts *
Author(s) -
Leroy J. G.,
O'Brien J. S.
Publication year - 1976
Publication title -
clinical genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 102
eISSN - 1399-0004
pISSN - 0009-9163
DOI - 10.1111/j.1399-0004.1976.tb01608.x
Subject(s) - galactoside , enzyme , beta galactosidase , beta (programming language) , biology , cell culture , microbiology and biotechnology , biochemistry , chemistry , escherichia coli , genetics , gene , computer science , programming language
A biochemical difference is found between the mucolipidoses II and III which may be correlated with their clinical phenotypes. In homogenates of mass‐cultured I‐cells from patients with MLII (I‐cell disease), the residual specific activity of beta‐galactosidase is between 3 and 5 times lower than that in the I‐cells from patients with MLIII (pseudo‐polydystrophy). This difference is confirmed in several covershlip culture experiments where conditions of inoculation, propagation, harvest and enzyme assays are rigidly controlled. MLIII cells also hydrolyse the natural substrates asialofetuin‐(H) 3 ‐galactoside and GM 1 ‐(H) 2 ‐galactoside more easily. This observation offers support to the hypothesis that beta‐galactosidase may play a role in the physiopathology of these mucolipidoses.