Documentation scienceplus.abes.fr version Bêta

À propos de : Overexpression, Purification, and in Vitro Refolding of the 11SGlobulin from Amaranth Seed in Escherichia coli        

AttributsValeurs
type
Is Part Of
Subject
Title
  • Overexpression, Purification, and in Vitro Refolding of the 11SGlobulin from Amaranth Seed in Escherichia coli
has manifestation of work
related by
Author
Abstract
  • An amarantin 11S globulin cDNA encoding one of the most important storage proteins of amaranthseeds, with a high content of essential amino acids, was expressed in Escherichia coli. A good levelof expression of recombinant amarantin with a molecular weight of 59 kDa was obtained. Therecombinant protein was extracted by ammonium sulfate precipitation and purified to homogeneityusing ion-exchange chromatography and reversed phase high-performance liquid chromatography.The expressed protein exhibited electrophoretic, immunochemical, and surface hydrophobicityproperties similar to those of native amarantin from amaranth seed. Also, the recombinant proteinwas refolded in vitro using two different methods. Keywords: Storage protein; amarantin; heterologous expression; recombinant amarantin; expressioninduction; immunodetection; in vitro refolding
article type
is part of this journal



Alternative Linked Data Documents: ODE     Content Formats:       RDF       ODATA       Microdata