組織の甲状腺ホルモン結合蛋白に関する研究:第4篇ラット肝の細胞性Thyroxine結合蛋白および細胞性Triiodothyronine結合蛋白の分離について

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Previous reports described the possibility of the purification of cellular thyroxine-and triiodothyronine binding proteins (C-T4BP and C-T3BP) by chromatography on diethylaminoethyl (DEAE) -cellulose, ammonium sulfate precipitation and gel filtration on Sephadex. It is the purpose of the peresent paper to describe the purification by large-scale chromatography on DEAE-cellulose and some properties of C-T4BP and C-T3BP from rat liver. Cellular T4BP was obtained in a partially purified form by directly chromatographing liver soluble proteins. Cellular T3BP was prepared in a partially purified form by ammonium sulfate precipitation and chromatography on DEAE-cellulose. The positions at which these proteins emerged from the DEAE-cellulose column were in accord with the previous results obtained by small-scale chromatography. Although sedimentation analyses of these preparations showed heterogeneity, the C-T4BP contained 73% of the protein with a sedimentation coefficient of 5.8S, while the C-T3BP contained 87% of the protein with a sedimentation coefficient of 5.4S. Both the C-T4BP and the C-T3BP were found to be non-diffusible into gel grains of Sephadex G-100, and therefore, they were considered to have molecular weights over 100,000.
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