Purification of recombinant LamB proteins using continuous elution electrophoresis: A comparison with immunoaffinity chromatography.

LamB is a membrane protein that allows the exposition of a foreign peptide on the surface of recombinant E. coli cells. An immunopurified hybrid 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 chromatography, to continuous elution electrophoresis, in the purification of two different hybrid LamB proteins expressing portions of gp160 and p17 HIV proteins as foreign epitopes. The results obtained showed that both methods yielded the same purification, although the electrophoretic procedure had a higher yield. Continuous-elution electrophoresis could be a useful tool for the purification of membrane proteins.