H. Ljungberg et al., EXPLOITATION OF A MONOCLONAL-ANTIBODY FOR WEAK AFFINITY-BASED SEPARATION IN CAPILLARY GEL-ELECTROPHORESIS, Electrophoresis, 19(3), 1998, pp. 461-464
Citations number
19
Categorie Soggetti
Biochemical Research Methods","Chemistry Analytical
Weak biospecific recognition has been established for affinity separat
ion in high performance liquid chromatography (HPLC). The use of weak
affinity chromatography (WAC) has been limited previously by the insuf
ficient separation efficiency achieved, allowing only some 1000 plates
/m to be obtained. However, it has been shown that chiral drug separat
ion can be performed with capillary affinity gel electrophoresis (CAGE
) at considerably improved efficiency as compared with traditional chr
omatographic procedures. Our present study demonstrates the potential
of weak affinity monoclonal antibodies as a generic method for immunol
ogically based separations in capillary electrophoresis. Monoclonal an
tibodies were polymerized within a silica capillary and were used for
the separation of structurally similar carbohydrate antigens. The resu
lts indicate that weak biospecific interactions can be utilized in a C
AGE format to produce highly selective separation of the alpha- and be
ta-forms of p-nitrophenyl-labeled maltose. It remains to be seen, howe
ver, how efficient weak affinity separation in CAGE can be compared wi
th affinity HPLC protocols. Details of typical separations and of the
preparation of the antibody gel are presented.