Expression of a lipocalin in prokaryote and eukaryote cells: Quantification and structural characterization of recombinant bovine beta-lactoglobulin

In this paper we quantify and characterize the expression of recombinant be ta-lactoglobulin (rBLG) in prokaryote and eukaryote cells. In Escherichia c oli we used the pET26 vector, which permits the secretion of rBLG in peripl asm, We studied the expression of rBLG in COS-7 cells and in vivo in mouse tibialis muscle. The expression of rBLG was measured by two immunoassays sp ecific, respectively, for BLG in its native and denatured conformation. We observed that rBLG was essentially expressed in a denatured form in E. coli even in the periplasm, whereas rBLG in eukaryote cells was found in its na tive conformation. (C) 1999 Academic Press.