Isolation and chemical and immunochemical characterization of the peanut-lectin-binding glycoprotein from human milk-fat-globule membranes

J. Fischer, P. J. Klein, G. H. Farrar, F. G. Hanisch, G. Uhlenbruck

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Abstract

Membrane glycoprotein with high M(r) (HM(r)-MGP) was purified from neuraminidase-treated Triton-100-solubilized human milk-fat-globule membranes by peanut-agglutinin (PNA) affinity chromatography. The high carbohydrate content (75%), blood-group-A activity and typical monosaccharide composition (L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosamine in the proportions 0.26:1.000:1.85:1.30) indicate that the isolated HM(r)-MGP is a mucinous substance. Fractionation of the oligosaccharides from alkaline-borohydride-treated HM(r)-MGP on Bio-Gel P-2 suggest that the PNA-binding sites are located mainly only longer (tetra- to deca-saccharide) alkali-labile bound oligosaccharide chains. Polyclonal antibodies raised against the HM(r)-MGP showed an antigenic distribution in histological sections that was comparable with the distribution of peroxidase-labelled-PNA-binding sites in both normal and malignant breast tissues. The positive immunohistological staining of some other tissue components with this antibody indicates that HM(r)-MGP is not strictly breast-associated. The functional role of HM(r)-MGP is unknown, but, since its expression is dependent on the differentiation state of secretory epithelial cells, it serves as a differentiation antigen that can be used for better functional characterization of breast cancers.

Original languageEnglish
Pages (from-to)581-589
Number of pages9
JournalBiochemical Journal
Volume224
Issue number2
DOIs
Publication statusPublished - Jan 1 1984

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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