Galactoside-binding lectin in human tissues

H. J. Allen, C. Karakousis, M. S. Piver, M. Gamarra, H. Nava, B. Forsyth, B. Matecki, A. Jazayeri, D. Sucato, E. Kisailus

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


Lactose-inhibitable lectin activity has been analyzed by hemagglutination assay in a variety of human tissues and cells obtained at surgery and autopsy. The lectin activity was detected in surgically removed melanoma, sarcoma, colon carcinoma, breast carcinoma, adjacent non-malignant tissues, non-malignant tissues obtained at autopsy and in cells isolated from malignant effusions. Although, on average, malignant tissue had a higher hemag-glutinating titer than non-malignant tissue, similar tissues from different individuals varied widely in their apparent lectin content. The lectin was isolated from lung by affinity chromatography and was found to have a native molecular mass of 31, 000 daltons and a subunit molecular mass of 14, 000 daltons. Utilizing rabbit anti-lung lectin serum in an immunohis-tochemical assay, the lectin was found to be distributed throughout the cytoplasm of lung epithelial cells. Ouchterlony immunodiffusion analysis confirmed the presence of this lectin in a variety of tissues and in some body fluids. In vitro metabolic radiolabelling experiments showed that the presence of lectin in tissues was most likely due to endogenous synthesis rather than absorption from body fluids. Lectin isolated from several tissues was found to bind to human buffy coat cell receptors.

Original languageEnglish (US)
Pages (from-to)218-229
Number of pages12
JournalTumor Biology
Issue number4
StatePublished - Jan 1 1987


  • Galactoside
  • Galaptin
  • Hemagglutinin
  • Lectin
  • Malignant

ASJC Scopus subject areas

  • Cancer Research


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