Separation of thyroxine(T4)-binding proteins of human serum in polyacrylamide gel at pH 7.4. I. Effect of pH on distrubution of tracer quantities of T4.
Separation of thyroxine(T4)-binding proteins of human serum in polyacrylamide gel at pH 7.4. I. Effect of pH on distrubution of tracer quantities of T4.
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在 pH 7.4 的聚丙烯酰胺凝胶中分离人血清的甲状腺素 (T4) 结合蛋白。
DOI:
10.1210/jcem-30-2-237
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发表时间:
1970
期刊:
影响因子:
--
通讯作者:
R. I. Gregerman
中科院分区:
文献类型:
--
作者:
P. Davis;R. I. Gregerman
ABSTRACT A polyacrylamide gel electrophoresis system buffered with piperazine-N,N′-bis-(2-ethane sulfonic acid) (PIPES) has been shown to be capable of resolving thyroxine-binding globulin (TBG), albumin and thyroxine-binding prealbumin (TBPA) at physiologic pH. In this system at tracer levels of thyroxine (T4), TBG binds 50% more T4 at pH 7.4 than at pH 9.0 (Tris-borate buffer). Inversely, binding of T4 by TBPA was reduced at physiologic pH but high at alkaline pH. The pH-dependence of TBPA binding confirms previously reported electrophoretic studies in agarose. The pH-dependence of T4 binding by the hormone-specific proteins explains in part disparities in binding data previously reported from various electrophoretic systems. Albumin binding of T4 was not substantially affected by changes of pH. Consistent, highly individualized post-TBG zone migration of T4 (range: 4–15%) was noted and was attributed to binding of hormone by proteins with relatively low affinities for thyroxine. Post-TBG zone binding o...