This work presents evidence on the association of active DDC molecules with
membranes in mammalian brain. L-DOPA decarboxylase (DDC) is generally cons
idered to be a cytosolic enzyme. Membrane-associated DDC was detected by im
munoblotting and enzymatic assay experiments. DDC activity and immunoreacti
vity could be partially extracted from mammalian brain membranes by deterge
nt. Fractionation of membranes by temperature-induced phase separation in T
riton X-114, resulted in the recovery of membrane-associated DDC in separat
ion phases where integral and hydrophobic membrane proteins separate. Treat
ment of membranes with phosphatidylinositol-specific phospholipase C or pro
teinase K, did not elute membrane-associated DDC activity, suggesting that
a population of DDC molecules exist embedded within membranes. The elucidat
ion of the functional significance of the enzyme's association with membran
es could provide us with new information leading to the better understandin
g of the biological pathways that DDC is involved in.