Expression, purification and characterization of soluble red rooster laforin as a fusion protein in Escherichia coli

Conclusions: Gg-laforin is more soluble and stable than human laforin in vitro, and possesses similar activity as a glucan phosphatase. Therefore, it can be used to model human laforin in structure-function studies. We have established a protocol for purifying recombinant Gg-laforin in sufficient quantity for crystallographic and other biophysical analyses, in order to better understand the function of laforin and define the molecular mechanisms of Lafora disease.
Source: BMC Biochemistry - Category: Biochemistry Authors: Source Type: research