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Protein Expr Purif. 2000 Apr;18(3):286-92.

Expression, purification, and characterization of histidine-tagged mouse monoglyceride lipase from baculovirus-infected insect cells.

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Section for Molecular Signalling, Lund University, Lund, S-221 00, Sweden.


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.

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