| Literature DB >> 10733881 |
M Karlsson1, H Tornqvist, C Holm.
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. Copyright 2000 Academic Press.Entities:
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Year: 2000 PMID: 10733881 DOI: 10.1006/prep.1999.1194
Source DB: PubMed Journal: Protein Expr Purif ISSN: 1046-5928 Impact factor: 1.650