Abstract
A sensitive hemagglutination test which uses simultaneously erythrocytes from two different species was developed to test the ability of glycosylated cytochemical markers to interact with membrane-bound lectins. The interaction between galactose-terminated glycoconjugates and Ricinus communis agglutinin 120 was chosen for exemplification. The lectin was covalently attached to the surface of sheep red blood cells, thus rendering them highly agglutinating for human erythrocytes. Small amounts of a large variety of terminal galactose-containing molecules inhibited the hemagglutination. The assay proved to be particularly useful for testing colloidal gold-adsorbed glycoconjugates of low protein concentration.
Original language | English (US) |
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Pages (from-to) | 503-509 |
Number of pages | 7 |
Journal | Analytical Biochemistry |
Volume | 148 |
Issue number | 2 |
DOIs | |
State | Published - Aug 1 1985 |
Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Keywords
- glutaraldehyde coupling
- glycoprotein-gold complexes
- glycosylated cytochemical markers
- hemagglutination
- immobilized lectins
- membrane lectins