These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: A comparison of the properties and bile salt specificities of galactosylceramide and lactosyl ceramide beta-galactosidase activities in human leucocytes and fibroblasts.
    Author: Poulos A, Beckman K.
    Journal: Clin Chim Acta; 1980 Feb 28; 101(2-3):277-85. PubMed ID: 6766828.
    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.
    [Abstract] [Full Text] [Related] [New Search]