SECRETION OF AN ACTIVE RECOMBINANT DOG GASTRIC LIPASE FROM BACULOVIRUS-INFECTED INSECT CELLS

An active dog gastric lipase (DGL) belonging to the acid-stable mammal ian lipase family, was produced and secreted from baculovirus-infected insect cells using the honeybee melittin and the DGL signal sequences . Both sequences drove the secretion of an active 47 kDa recombinant D GL (rDGL). rDGL was secreted at about 35 mg/L of culture medium. A one step purification using a cation exchange chromatography was used to recover an active electrophoretically pure rDGL from 2 days post-infec tion supernatant. There were not significant differences between the e nzymatic properties of native and recombinant proteins.