Estimation of biotinylated lectin by isoelectric focusing
- 1 January 1990
- journal article
- research article
- Published by Wiley in Electrophoresis
- Vol. 11 (6) , 505-506
- https://doi.org/10.1002/elps.1150110613
Abstract
Concanavalin A (Con A) was biotinylated to various degrees using N‐biotinyl‐ω‐aminocaproic‐acid‐N‐hydroxy succinimide ester as the biotinylation reagent, and then analyzed by isoelectric focusing using PhastGel IEF 3–9. The isoelectric points of biotinylated ConAs were found to decrease with increasing concentration of the biotinylation reagent. Analysis by isoelectric focusing followed by dot blotting clearly indicated that the biotinylated ConA with an isoelectric point lower than that of the original ConA by 2.2 ± 0.6 had the strongest binding activity for ovalbumin.This publication has 5 references indexed in Scilit:
- Fast horizontal electrophoresis. I. Isoelectric focusing and polyacrylamide gel electrophoresis using PhastSystem™Electrophoresis, 1988
- Ligands for insulin receptor isolationBiochemistry, 1984
- [12] The ultrastructural visualization of cell surface glycoconjugatesPublished by Elsevier ,1982
- Specificity, stereochemistry, and mechanism of the color reaction between p-dimethylaminocinnamaldehyde and biotin analogsAnalytical Biochemistry, 1970
- A Spectrophotometric Assay for Avidin and Biotin Based on Binding of Dyes by AvidinBiochemical Journal, 1965