Lectin binding affinities of human milk fat globule (HMFG) membrane antigens.
Six biotinylated lectins with differing specificities and two monoclonal antibodies (III D 5 and III H 2) were used to characterize the sugar-residues in human milk fat globule (HMFG) membrane antigens. Immunoblotting analysis revealed that most of the antigens contain several sugars. However, the molecules exclusively reacting with anti-HMFG III D 5, a monoclonal antibody previously shown to detect antigen(s) positively correlating with the expression of estrogen receptors in mammary and gynaecological carcinomas, could only be stained with peanut agglutinin and Ricinus communis-lectins. One of these antigens, a 42-57 kDa molecule, was shown to have a complexed quaternary structure with galactose determining the antigenic specificity. It is suggested that the production of this glycoprotein in estrogen sensitive tissues results from activation of galactosyl-transferase-enzyme at the same time as the expression of estrogen receptors.
Ashorn
P
P
Vilja
P
P
Ashorn
R
R
Krohn
K
K
D001667:Binding, Competitive; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes; D006801:Humans; D037102:Lectins / Q000276:immunology*; D008565:Membrane Proteins / Q000276:immunology*; D008895:Milk, Human / Q000276:immunology*; D018396:Mucin-1; D013194:Staining and Labeling
D000939:Epitopes; D037102:Lectins; D008565:Membrane Proteins; D018396:Mucin-1