Biochemical characterisation studies on a leukocyte alloantigen expressed with high frequency in leukaemia patients.
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.
Weedle
R M
RM
Department of Biology, St Patrick's College, Kildare, Republic of Ireland.
Cotter
T G
TG
D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm / Q000032:analysis*; D006026:Glycoside Hydrolases / Q000494:pharmacology; D006801:Humans; D007519:Isoantigens / Q000032:analysis*; D007938:Leukemia / Q000276:immunology*; D007962:Leukocytes / Q000276:immunology*; D008970:Molecular Weight; D011233:Precipitin Tests
D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm; D007519:Isoantigens; D006026:Glycoside Hydrolases