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 Damino 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 CD spectroscopy. A figure of 70mg of pure protein per liter of fermentation broth was achieved.
|Data di pubblicazione:||2006|
|Titolo:||Expression in Escherichia coli and in vitro refolding of the human protein pLG72|
|Rivista:||PROTEIN EXPRESSION AND PURIFICATION|
|Codice identificativo ISI:||WOS:000235902700019|
|Codice identificativo Scopus:||2-s2.0-32644480821|
|Appare nelle tipologie:||Articolo su Rivista|