Colloidal properties of human transferrin receptor in detergent free solution.
The colloidal properties of transferrin receptor, isolated from human placenta, in detergent free solution has been investigated by light scattering techniques and analytical ultracentrifugation. In detergent free solution at 293.2 K, hTfR forms stable aggregates with an apparent hydrodynamic radius of 17 nm. The molecular mass was determined by ultracentrifugation to lie between (1722+/-87) kDa (sedimentation equilibrium) and (1675+/-46) kDa (sedimentation velocity). This implies that the aggregates are build up from nine hTfR dimers. Based on model calculations, which are in good agreement with the experimental data, we propose a torus-like structure for the aggregates. Upon pH shift from pH 7.5 to 5.0 or removal of the N-linked carbohydrate chains, formation of larger aggregates is induced. These aggregates can be described in terms of porous fractal structures. We propose a simple model, which accounts for that behaviour assuming that the aggregation is mainly due to the reduction of negative surface charge.
Schüler
J
J
Institut für Kristallographie, Freie Universität Berlin, Takustrasse, Berlin, Germany.
Frank
J
J
Behlke
J
J
Saenger
W
W
Georgalis
Y
Y
D002942:Circular Dichroism; D003102:Colloids; D003902:Detergents / Q000737:chemistry; D006801:Humans; D011487:Protein Conformation; D011990:Receptors, Transferrin / Q000737:chemistry*
D003102:Colloids; D003902:Detergents; D011990:Receptors, Transferrin