| Title : Expression, purification, and characterization of histidine-tagged mouse monoglyceride lipase from baculovirus-infected insect cells - Karlsson_2000_Protein.Expr.Purif_18_286 |
| Author(s) : Karlsson M , Tornqvist H , Holm C |
| Ref : Protein Expr Purif , 18 :286 , 2000 |
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Abstract :
Monoglyceride lipase (MGL) has been produced with the baculovirus-insect cell system. The mouse MGL cDNA was subcloned into a baculovirus transfer vector in frame with a sequence encoding an N-terminal stretch of six histidine residues. Purification to apparent homogeneity was obtained by nickel-chelating chromatography. The final yield was 3 mg of pure enzymatically active MGL per liter of Sf9 cell suspension culture. Analysis by SDS-PAGE and mass spectrometry showed that the recombinant histidine-tagged enzyme had the expected molecular mass. With monoolein as substrate, the specific activity and the apparent K(m) were close to those of rat MGL of adipose tissue. |
| PubMedSearch : Karlsson_2000_Protein.Expr.Purif_18_286 |
| PubMedID: 10733881 |
Karlsson M, Tornqvist H, Holm C (2000)
Expression, purification, and characterization of histidine-tagged mouse monoglyceride lipase from baculovirus-infected insect cells
Protein Expr Purif
18 :286
Karlsson M, Tornqvist H, Holm C (2000)
Protein Expr Purif
18 :286