G. Flamminio et al., PURIFICATION OF RECOMBINANT LAMB PROTEINS USING CONTINUOUS ELUTION ELECTROPHORESIS - A COMPARISON WITH IMMUNOAFFINITY CHROMATOGRAPHY, Biochemistry and molecular biology international, 36(6), 1995, pp. 1255-1261
LamB is a membrane protein that allows the exposition of a foreign pep
tide on the surface of recombinant E. coli cells. An immunopurified hy
brid LamB protein has been used to elicit hight-titre antibodies to a
foreign epitope. Looking for a simpler purification procedure we have
compared the traditional approach, which includes affinity chromatogra
phy, to continuous elution electrophoresis, in the purification of two
different hybrid LamB proteins expressing portions of gp160 and p17 H
IV proteins as foreign epitopes. The results obtained showed that both
methods yielded the same purification, although the electrophoretic p
rocedure had a higher yield. Continuous-elution electrophoresis could
be a useful tool for the purification of membrane proteins.