A quantitative assay for concanavalin A- and Ricinus communis agglutinin-mediated agglutinations of rat ascites hepatoma cellsRelationship between concanavalin a binding and cell agglutination
Autor: | Isao Kaneko, Hikoya Hayatsu, Tyunosin Ukita |
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Rok vydání: | 1975 |
Předmět: |
Carcinoma
Hepatocellular Time Factors Cell Biophysics Biology Biochemistry Agglutinin Agglutination Tests Lectins Concanavalin A Methods medicine Animals Binding site Receptor Molecular Biology Ricinus Liver Neoplasms Neoplasms Experimental biology.organism_classification Molecular biology Rats Kinetics Plants Toxic Agglutination (biology) medicine.anatomical_structure biology.protein Binding Sites Antibody Plant Lectins Antibody Mathematics Protein Binding |
Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 392:131-140 |
ISSN: | 0304-4165 |
Popis: | A simple quantitative assay method was developed for the agglutination of rat ascites hepatoma cells mediated by Concanavalin A or Ricinus communis agglutinin. This method was based on the principle that the turbidity of a cell suspension is proportional to the sum of the cross-sectional area of cells and aggregatesmas predicted by the theoretical consideration, the turbidity decreased when cells were aggregated and the decrease was a function of the average number of the cells in aggregates. The agglutinability of the cells, judged by this method, showed a maximum value at a certain concentration of the agglutinin. By further addition of the agglutinin, the agglutinability slightly decreased from the maximum. These phenomena were observed both for Concanavalin A and Ricinus communis agglutinin. The binding and the agglutination experiments using [3-H]concanavalin A revealed that the binding to approx;0% of the total receptors caused a maximal agglutination. This suggested that the receptors responsible for the agglutination constitute only a small part of the total receptors on the surface. |
Databáze: | OpenAIRE |
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