Purification and crystallisation of the autoantigen thyroid peroxidase from human Graves' thyroid tissue

Biochemical and Biophysical Research Communications
A GardasJ P Banga

Abstract

Milligram quantities of the human membrane autoantigen thyroid peroxidase (TPO) have been purified to a high degree of homogeneity by a combination of detergent solubilisation, monoclonal antibody affinity, and ion exchange chromatography, from pooled Graves' disease thyroid glands. The purified TPO of greater than 90% purity was enzymatically active as judged by its ability to oxidise guaiacol. Crystals of TPO have been grown from solutions of the protein solubilised in sodium deoxycholate, in the presence of ammonium sulphate. The crystals exhibited birefringence under polarised light, indicative of molecular order. Crystallisation of this large, membrane autoantigen represents the first step in delineating the complete three-dimensional structure of a human autoantigen involved in destructive thyroiditis.

Citations

Sep 8, 2007·Thyroid : Official Journal of the American Thyroid Association·Sandra M McLachlan, Basil Rapoport
Sep 20, 2000·Redox Report : Communications in Free Radical Research·A GardasJ P Banga
Apr 29, 2015·Biochimica Et Biophysica Acta·Ying-Wu Lin
Dec 29, 2000·International Reviews of Immunology·S M McLachlan, B Rapoport
Dec 13, 2003·Autoimmunity·Takashi Akamizu
Feb 7, 2018·Archives of Biochemistry and Biophysics·William M Nauseef
Aug 16, 2005·Archives of Biochemistry and Biophysics·Jean Ruf, Pierre Carayon
Mar 17, 2005·Journal of Autoimmune Diseases·Damien BressonSylvie Péraldi-Roux

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