Journal
PROTEIN EXPRESSION AND PURIFICATION
Volume 18, Issue 3, Pages 286-292Publisher
ACADEMIC PRESS INC
DOI: 10.1006/prep.1999.1194
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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. (C) 2000 Academic Press.
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