Abstract
In this report we describe, using a previously characterised monoclonal antibody (NC-2), the biochemical characteristics of a human leukaemia-associated alloantigen. Two proteins with molecular weights of 50 kDa and 15 kDa were immunoprecipitated from 125I surface labelled HL-60 cells. Both proteins appeared to be sensitive to digestion with trypsin, the 50 kDa protein in particular. Treatment with glycopeptidase F indicated the presence of N-linked oligosaccharides, whereas treatment with neuraminidase had no effect on the mobility of the antigens in SDS-PAGE indicating the absence of detectable sialic acid residues. Sensitivity to glycopeptidase F indicates that the reacting antigens are glycoproteins in nature. The antibody reacts with a range of normal tissues and appears to be associated with cytoplasmic granules in HL-60 cells.
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.
