Limulus polyphemus lectin sites in human bronchial mucosa.
Open Access
- 1 June 1977
- journal article
- research article
- Published by SAGE Publications in Journal of Histochemistry & Cytochemistry
- Vol. 25 (6) , 470-473
- https://doi.org/10.1177/25.6.328765
Abstract
The lectin from Limulus polyphemus (limulin) has an affinity for glycoproteins containing N-glycolyl or N-acetylneuraminic residues. By using a peroxidase labeled limulin on human bronchial mucosa sections, it has been possible to demonstrate selectively a diffuse staining within the apical part of the epithelial goblet cells. Whereas, in the submucosal glands serous cells, the labeling appears as small granules localized either at the apical pole or in the whole cytoplasm. In our experimental conditions the labeled limulin has no affinity for mucous cells that are known to contain sialic acid residues.This publication has 2 references indexed in Scilit:
- Clinica Chimica Acta; International Journal of Clinical Chemistry, 1976
- THF EARLY STAGES OF ABSORPTION OF INJECTED HORSERADISH PEROXIDASE IN THE PROXIMAL TUBULES OF MOUSE KIDNEY: ULTRASTRUCTURAL CYTOCHEMISTRY BY A NEW TECHNIQUEJournal of Histochemistry & Cytochemistry, 1966