Lectin-enzyme immunoassay of transferrin sialovariants using immobilized antitransferrin and enzyme-labeled galactose-binding lectin from Ricinus communis
✍ Scribed by J.M. Pekelharing; P. Vissers; H.A. Peters; B. Leijnse
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 581 KB
- Volume
- 165
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
A heterologous lectin-enzyme immunoassay is described. Microtiter plate wells were coated with affinity-purified antibodies to human transfenin. After incubation with transferrin sialovariants, prepared by limited neuraminidase treatment and separated with chromatofocusing, a lectin-enzyme-streptavidin complex was added. A good correlation was obtained between the number of terminal galactose groups on transferrin and the response in the lectin-enzyme immunoassay using Ricinus communis agglutinin as the galactose-binding lectin. The results indicate that characterization of glycosylation is possible with less than a microgram of the glycoprotein available, using lectin-enzyme immunoassays.