Expression of recombinant cyclooxygenase 1 in Drosophila melanogaster S2 cells transformed with human [beta]1,4-galactosyltransferase and Gal[beta]1,4-GlcNAc [alpha]2,6-sialyltransferase

We examined the expression of human cyclooxygenase-1 (COX-1) in Drososphila melanogaster S2 (S2) cells transformed with cDNAs encoding β1,4-galactosyltransferase (GalT) and Galβ1,4-GlcNAc α2,6-sialyltransferase (ST). Southern blot analysis indicated that multiple copies of the glycosyltransferases genes were integrated into the S2 cell genome. A lectin blot analysis also indicated that recombinant COX-1 from S2COX-1/GalT-ST cells contained the glycan residues of β1,4-linked galactose and α2,6-linked sialic acid. The specific peroxidase activity of recombinant sialylated COX-1 from S2COX-1/GalT-ST cells was 41,250 U mg^sup -1^, indicating an increase of approximately 22% compared with a non-sialylated control (33,850 U mg^sup -1^) from S2COX-1 cells.[PUBLICATION ABSTRACT]