G. Joliff et al., SECRETION OF AN ACTIVE RECOMBINANT DOG GASTRIC LIPASE FROM BACULOVIRUS-INFECTED INSECT CELLS, Biotechnology letters, 20(7), 1998, pp. 697-702
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.