Production and purification of recombinant human hepcidin-25 with authentic N and C-termini
GARBAY, Bertrand
Biotechnologie des protéines recombinantes à visée santé
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
< Réduire
Biotechnologie des protéines recombinantes à visée santé
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
Langue
en
Article de revue
Ce document a été publié dans
Journal of Biotechnology. 2015, vol. 195, p. 89-92
Elsevier
Résumé en anglais
Hepcidin was first identified as an antimicrobial peptide present in human serum and urine. It was later demonstrated that hepcidin is the long-sought hormone that regulates iron homeostasis in mammals. Recombinant human ...Lire la suite >
Hepcidin was first identified as an antimicrobial peptide present in human serum and urine. It was later demonstrated that hepcidin is the long-sought hormone that regulates iron homeostasis in mammals. Recombinant human Hepcidin-25 (Hepc25) was expressed in Pichia pastoris using a modified version of the pPICZ alpha A vector. Hepc25 was then purified by a simple two-step chromatographic process to obtain 1.9 mg of soluble recombinant human Hepc25 per liter of culture at 96% purity. The sequence of Hepc25 and the presence of four disulfide bridges were confirmed by mass spectrometry analyses, and the recombinant Hepc25 exhibited antibacterial activity. This protocol of production and purification is the first step toward the production of human Hepc25 at a greater scale. (C) 2015 Elsevier B.V. All rights reserved.< Réduire
Mots clés en anglais
IMAC
Hepcidin
P. pastoris
Recombinant expression
Expanded bed adsorption
Origine
Importé de halUnités de recherche