Histochemical lectin affinity technique by means of FITC-labeled serum protein fractions
- 1 January 1976
- journal article
- research article
- Published by Springer Nature in Histochemistry and Cell Biology
- Vol. 49 (1) , 67-72
- https://doi.org/10.1007/bf00490127
Abstract
A two-step affinity technique is described for light microscopic demonstration of the Concanavalin A, Agaricus bisporus lectin and Ricinus communis lectin binding sites by means of various FITC-labeled human and rabbit serum protein fractions. Experiments for the visualization of the Lens culinaris lectin and the Pisum sativum lectin binding sites gaves negative results. The technique consist of two reaction steps which involve the incubation of tissue sections in the lectins followed by the visualization of receptor-bound lectins with FITC-labeled serum protein fractions basing on their carbohydrate content. The specificity of the technique could be demonstrated by the addition of the hapten or by incubation in the FITC-labeled serum protein fractions only. In contrast to the direct or indirect staining methods only very small amounts of purified lectins are necessary.Keywords
This publication has 23 references indexed in Scilit:
- Wheat germ agglutinin and Ricinus communis agglutinin as specific saccharide stains in light and electron microscopyExperimentelle Pathologie, 1975
- Light and electron microscopic demonstration ofd-mannose andd-glucose like sites at the cell surface by means of the lectin from theLens culinarisCellular and Molecular Life Sciences, 1974
- AN IMMUNOFLUORESCENT TECHNIQUE FOR OBSERVING THE BINDING OF CONCANAVALIN A TO FROZEN TISSUE SECTIONSJournal of Histochemistry & Cytochemistry, 1973
- The interaction of Ricinus communis agglutinin with normal and tumor cell surfacesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1972
- Purification of galactose-binding phytoagglutinins and phytotoxin by affinity column chromatography using sepharoseCellular and Molecular Life Sciences, 1972
- Ultrastructural visualization of cellular carbohydrate components by means of concanavalin AExperimental Cell Research, 1971
- Some properties of purified phytohemagglutinin from Lens culinaris seedsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- Studies on phytohemagglutinins III. Isolation and characterization of hemagglutinins from the pea (Pisum sativum L.)Biochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- Isolation and characterization of a phytohemagglutinin from the lentilBiochemistry, 1969
- Specific Protein of Legumes which reacts with Animal ProteinsNature, 1960