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蛋白质分子的表观电荷。人甲状腺素结合蛋白。

Apparent electric charge of protein molecules. Human thyroxine - binding proteins.

作者信息

Hocman G, Sadlon J

机构信息

Research Institute of Human Bioclimatology, Experimental Gerontology Unit, and Institute of Experimental Endocrinology, Slovak Academy of Sciences, Bratislava, Czechoslowakia.

出版信息

Biochem Exp Biol. 1977;13(4):381-3.

PMID:16296167
Abstract
  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.
摘要
  1. 通过在相同条件下比较两种不同带电粒子的电泳迁移率,当已知另一个粒子的电荷时,就可以计算出一个粒子的净基本静电荷。2. 人甲状腺素结合球蛋白的电泳迁移率在0.05至0.20摩尔范围内不依赖于Tris - HCl缓冲液的浓度。在pH 7.0和8.6时,该迁移率的值分别为0.078和0.083 cm² vol⁻¹ hour⁻¹。3. 在弱碱性溶液中,人甲状腺素结合球蛋白的净基本静电荷似乎约为22个负基本静电单位。

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