An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines

► Tetanus toxoid important conjugation for carbohydrate vaccines. ► Physical nature in solution needs elucidating. ► Sedimentation velocity shows small (∼14%) dimerization. ► Dimers not in reversible equilibrium. ► Overall asymmetric conformation. Tetanus toxoid protein has been characterized with r...

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Veröffentlicht in:	Carbohydrate polymers 2012-11, Vol.90 (4), p.1831-1835
Hauptverfasser:	Abdelhameed, Ali Saber, Morris, Gordon A., Adams, Gary G., Rowe, Arthur J., Laloux, Olivier, Cerny, Louis, Bonnier, Benjamin, Duvivier, Pierre, Conrath, Karel, Lenfant, Christophe, Harding, Stephen E.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical ultracentrifugation Analytical, structural and metabolic biochemistry Applied sciences Biological and medical sciences Chromatography, Gel Exact sciences and technology Fundamental and applied biological sciences. Psychology Glycoconjugates Hydrodynamics Miscellaneous Molecular Weight Natural polymers Physicochemistry of polymers polysaccharides Protein Multimerization Proteins Scattering, Small Angle Solution conformation surface area tetanus Tetanus Toxoid - chemistry Ultracentrifugation vaccines Vaccines, Conjugate - chemistry viscometry Viscosity
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