Partition of T4 to plasma proteins is classically attributed only to TBGC (≈70%), transthyretin (≈15%) and albumin (≈10%), based on zone electrophoresis. Since TBG migration spans the α1 and α2 regions, and since HDL, which have α1 migration, transport ≈4% of circulating T4, other α-globulins could bind T4 and "contaminate" the TBG area. Hence, we determined the association of [125I]T4 to TBG and, for comparison, to transthyretin and albumin. Sera from 50 normolipidemic individuals were equilibrated with [125I]T4 and analyzed by both zone electrophoresis and radioimmunoprecipitation with specific antisera. Transthyretin-T4 or albumin-T4 bindings as assessed by the two methods agreed, while TBG-T4 did not, because other α-globulins carrying T4 with low affinity co-migrated with TBG. Some, but not all, of these α-globulins belong to the same superfamily of TBG and also bind steroid hormones. ©2002, Editrice Kurtis.
Thyroxine binding to members and non-members of the serine protease inhibitor family
BENVENGA, Salvatore;TRIMARCHI, Francesco
2002-01-01
Abstract
Partition of T4 to plasma proteins is classically attributed only to TBGC (≈70%), transthyretin (≈15%) and albumin (≈10%), based on zone electrophoresis. Since TBG migration spans the α1 and α2 regions, and since HDL, which have α1 migration, transport ≈4% of circulating T4, other α-globulins could bind T4 and "contaminate" the TBG area. Hence, we determined the association of [125I]T4 to TBG and, for comparison, to transthyretin and albumin. Sera from 50 normolipidemic individuals were equilibrated with [125I]T4 and analyzed by both zone electrophoresis and radioimmunoprecipitation with specific antisera. Transthyretin-T4 or albumin-T4 bindings as assessed by the two methods agreed, while TBG-T4 did not, because other α-globulins carrying T4 with low affinity co-migrated with TBG. Some, but not all, of these α-globulins belong to the same superfamily of TBG and also bind steroid hormones. ©2002, Editrice Kurtis.Pubblicazioni consigliate
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