PURIFICATION OF RECOMBINANT LAMB PROTEINS USING CONTINUOUS ELUTION ELECTROPHORESIS - A COMPARISON WITH IMMUNOAFFINITY CHROMATOGRAPHY

Citation
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
Citations number
18
Categorie Soggetti
Biology
ISSN journal
10399712
Volume
36
Issue
6
Year of publication
1995
Pages
1255 - 1261
Database
ISI
SICI code
1039-9712(1995)36:6<1255:PORLPU>2.0.ZU;2-2
Abstract
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.