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• W2013456314 abstract "The properties and bile salt specificities of galactosylceramide and lactosylceramide beta-galactosidase activities (GC and LC-beta-galactosidases) of human leucocytes and fibroblasts were compared. A number of differences were observed. Under the standard assay conditions the former activity was more sensitive to Zn2+ and Triton-X100. Glycocholate and cholate were more active stimulators of the GC-beta-galactosidase than the more frequently used taurocholate which was the most effective stimulator of LC-beta-galactosidase activity. It is postulated that some of the apparent differences in the properties of GC- and LC-beta-galactosidase activities may be attributed to the different micellar properties of the lipid substrates. Experiments with fibroblasts from patients with Krabbe's disease confirmed an almost total absence of GC-beta-galactosidase whichever bile acid was employed. Residual LC-beta-galactosidase activity detected in these cells was much higher ranging from 13% of the lowest measured value when measured with taurocholate to approximately normal values with glycocholate. Fibroblasts obtained from patients with GM1-gangliosidosis displayed close to normal GC and LC-beta-galactosidase activity under our experimental conditions. The data suggest that diagnoses of Krabbe's disease should be performed with galactosylceramide rather than lactosylceramide as substrate." @default.
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• W2013456314 date "1980-02-01" @default.
• W2013456314 modified "2023-09-23" @default.
• W2013456314 title "A comparison of the properties and bile salt specificities of galactosylceramide and lactosyl ceramide β-galactosidase activities in human leucocytes and fibroblasts" @default.
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• W2013456314 doi "https://doi.org/10.1016/0009-8981(80)90254-5" @default.
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