Quantitative analysis methods have allowed scientists to create the first procedure for expressing the full-length recombinant diacylglycerol acyltransferases (DGAT1).
DGATs catalyze the final and rate-limiting step of triacylglycerol (TAG) biosynthesis in eukaryotic organisms, however while database research has identified 59 DGAT1 sequences from 48 organisms, the expression of any DGAT1 as a full-length protein in E.coli has never been revealed.
This is thought to be because DGAT1s are integral membrane proteins and, as such, are difficult to express and purify.
However, using amylose resin affinity chromatography and other quantitative analysis methods in a study published by BMC Biotechnology, researchers from the US Department of Agriculture identified a way to express the full-length recombinant DGAT1 from any species using a bacterial expression system.
"Although the protein was not purified to homogeneity in the current study, the ability to express full-length DGAT1 in E. coli could provide the basis for future purification of the protein," the study claimed.
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