We expressed a guinea pig 11 beta-hydroxylase cDNA (1) in COS-1 cells.
In order to find the optimal expression system we compared three expr
ession plasmids, each driven by a different promoter. Although promote
rs exhibited different transcriptional activities this did not result
in different enzymatic activities. Upon cotransfection with bovine adr
enodoxin a 5-fold increase of enzyme activity was achieved. A comparis
on with the bovine 11 beta-hydroxylase clearly demonstrated that the g
uinea pig enzyme was not able to produce significant amounts of 18-hyd
roxylated and 18-oxidized products from deoxycorticosterone under the
experimental conditions used.