Recently, genes coding for pLG72 and D-amino acid oxidase have been related to schizophrenia, a widespread psychiatric disorder that affects about 1% of population. pLG72 is a puzzling, novel protein present only in primates and proposed to be an activator of D-amino acid oxidase. Here we report on the overexpression of wild-type and His-tagged pLG72 in Escherichia coli. Both variants form inclusion bodies and have been refolded and purified to homogeneity: the acquisition of secondary and tertiary structure was demonstrated by CID spectroscopy. A figure of similar to 70 mg of pure protein per liter of fermentation broth was achieved. (c) 2005 Elsevier Inc. All rights reserved.