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Estimation of biotinylated lectin by isoelectric focusing
Author(s) -
Harada Hiroshi,
Kondo Maki,
Yamaguchi Takashi
Publication year - 1990
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150110613
Subject(s) - biotinylation , isoelectric point , isoelectric focusing , concanavalin a , chromatography , chemistry , lectin , biotin , reagent , biochemistry , enzyme , organic chemistry , in vitro
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.