Biochemical and Immunohisto-Chemical Characterization of a Peanut Agglutinin Binding Glycoprotein in Normal and Malignant Breast Tissues

Abstract PNA affinity chromatography was used to isolate the receptor molecules of this lectin from neuraminidase-treated, Triton X-100 solubilized human milk fat globule membranes (MPGM). The purified high molecular weight (HMW) glycoprotein contained about 70 – 75 % carbohydrate, with fucose (5.5 %), galactose (20.5 %), N-acetyl-galactosamine (33 %), N-acetyl-glucosamine (40 %) and only traces of other hexoses in their carbohydrate moiety. Antibodies raised against this mucus type glycoprotein showed a histological distribution in normal and malignant breast tissues, which was comparable to the distribution of the binding sites of the PNA-lectin and some monoclonal antibodies produced by immunization with the whole MFGMs.