Abstract
The glycosylation of β-hexosaminidase was investigated in the transformed cell-line, CCRF/CEM, derived from a human acute lymphoblastic leukaemia, and comparisons were made with enzyme from normal human skin fibroblasts. A series of studies including neuraminidase sensitivity, lectin chromatography, Biogel P4 chromatography of [ 3H]-mannose-labelled glycopeptides and endoglycosidase susceptibility, provided clear evidence that in CCRF/CEM cells, β-hexosaminidase was abnormally glycosylated. The results indicate that leukaemia-associated changes in β-hexosaminidase expression are probably due to increased sialylation of highly-branched complex oligosaccharides.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
