Apparent electric charge of protein molecules. Human thyroxine - binding proteins.
1. By comparison of electrophoretic mobilities of two different charged particles under the same conditions the net elementary electrostatic charge of one particle could be calculated when the charge of the other is known. 2. The electrophoretic mobility of human thyroxine - binding globulin does not depend upon the concentration of Tris - HCl buffer in the range 0.05 to 0.20 molar. The value of this mobility is 0.078 and 0.083 cm2 vol(-1) hour(-1) at pH 7.0 and 8.6, respectively. 3. The net elementary electrostatic charge of the human thyroxine - binding globulin appears to be approximately 22 negative elementary electrostatic units in mild alkaline solutions.
Hocman
G
G
Research Institute of Human Bioclimatology, Experimental Gerontology Unit, and Institute of Experimental Endocrinology, Slovak Academy of Sciences, Bratislava, Czechoslowakia.
Sadlon
J
J
D004563:Electrochemistry; D004590:Electrophoresis, Paper; D006801:Humans; D006863:Hydrogen-Ion Concentration; D013975:Thyroxine-Binding Proteins / Q000737:chemistry*
D013975:Thyroxine-Binding Proteins