In vitro triiodothyronine binding to cytoplasmic proteins from human red blood cells. |
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| Authors: | J Michelot B Dastugue N Defer G Meyniel |
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| Institution: | 3. INSERM U 71, BP 184 63005 Clermont-Ferrand, France;12. Laboratoire de Biochimie, Faculté de Médecine, 63001 Clermont-Ferrand, France;123. Institut de Pathologie Moléculaire, Faculté de Médecine Cochin, 75014 Paris, France |
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| Abstract: | In vitro incubations of cytosol proteins from human red blood cells with 125I] labelled L-3,5,3′ triiodothyronine demonstrated the existence of high affinity and limited capacity binding sites for T3. At 4°C, the rate constant of association was 3 × 107 M?1h?1, and the rate constant of dissociation was 9.10?3h?1. The dissociation constant Kd was calculated from these data or measured by Scatchard analysis and found to be between 3 and 7.10?10M. The maximum binding capacity was 1.4 f moles of L-3,5,3′ triiodothyronine per mg cytosol proteins. A close parallel between the biological pontency of the analogs of L-T3 was observed. |
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| Keywords: | L-thyroxine L-3 5 3′ triiodothyronine TETRAC 3 3′ 4 5′-tetraiodothyroacetic acid TRIAC 3 5 3′-triiodothyroacetic acid MIT L-monoiodotyrosine DIT L-diiodotyrosine TBG thyroxine binding globuline RBC red blood cells |
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