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Molecular interconversion of cold-sensitive cytosolic 3,3',5-tri-iodo-L-thyronine-binding proteins from human erythrocytes: effect of cold, heat and pH treatments.人红细胞中冷敏感胞质3,3',5-三碘-L-甲状腺原氨酸结合蛋白的分子互变：冷、热和pH处理的影响
Biochem J. 1993 Mar 1;290 ( Pt 2)(Pt 2):579-82. doi: 10.1042/bj2900579.
2
Novel cold-sensitive cytosolic 3,5,3'-triiodo-L-thyronine-binding proteins in human red blood cell. Isolation and characterization.人类红细胞中新型冷敏性胞质3,5,3'-三碘-L-甲状腺原氨酸结合蛋白。分离与鉴定。
J Biol Chem. 1991 Sep 5;266(25):16415-9.
3
Cold-sensitive cytosolic 3,5,3'-triiodo-L-thyronine-binding protein and pyruvate kinase from human erythrocytes share similar regulatory properties of hormone binding by glycolytic intermediates.
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Changes in cytosolic 3,5,3'-tri-iodo-L-thyronine (T3) binding activity during administration of L-thyroxine to thyroidectomized rats: cytosolic T3-binding protein and its activator act as intracellular regulators for nuclear T3 binding.甲状腺切除大鼠给予左旋甲状腺素期间胞质3,5,3'-三碘-L-甲状腺原氨酸（T3）结合活性的变化：胞质T3结合蛋白及其激活剂作为核T3结合的细胞内调节剂。
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Cytosolic 3,5,3'-triiodo-L-thyronine (T3)-binding protein (CTBP) regulation of nuclear T3 binding: evidence for the presence of T3-CTBP complex-binding sites in nuclei.
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Purification of cytosolic 3,5,3'-triiodo-L-thyronine(T3)-binding protein(CTBP) which regulates nuclear T3 translocation.调节核三碘甲状腺原氨酸（T3）转运的胞质3,5,3'-三碘-L-甲状腺原氨酸（T3）结合蛋白（CTBP）的纯化。
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引用本文的文献

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Differential effect of triiodothyronine and thyroxine on liposomes containing cholesterol: physiological speculations.三碘甲状腺原氨酸和甲状腺素对含胆固醇脂质体的不同作用：生理学推测
J Membr Biol. 1995 Sep;147(2):217-21. doi: 10.1007/BF00233549.

本文引用的文献

1
Concentrations of thyroxine and 3,5,3'-triiodothyronine at 34 different sites in euthyroid rats as determined by an isotopic equilibrium technique.采用同位素平衡技术测定正常甲状腺功能大鼠34个不同部位甲状腺素和3,5,3'-三碘甲状腺原氨酸的浓度。
Endocrinology. 1985 Sep;117(3):1201-8. doi: 10.1210/endo-117-3-1201.
2
Characterization of triiodothyronine transport and accumulation in rat erythrocytes.大鼠红细胞中三碘甲状腺原氨酸转运与蓄积的特性研究
Endocrinology. 1988 Nov;123(5):2303-11. doi: 10.1210/endo-123-5-2303.
3
Effects of human thyroxine-binding globulin and prealbumin on the reverse flow of thyroid hormones from extravascular space into the bloodstream in rabbits.人甲状腺素结合球蛋白和前白蛋白对兔甲状腺激素从血管外间隙逆向流入血液的影响。
Endocrinology. 1989 Mar;124(3):1428-37. doi: 10.1210/endo-124-3-1428.
4
Erythrocyte-associated triiodothyronine in the rat: a source of hormone for target cells.大鼠红细胞相关的三碘甲状腺原氨酸：靶细胞的激素来源。
Acta Endocrinol (Copenh). 1990 Mar;122(3):341-8. doi: 10.1530/acta.0.1220341.
5
Evidence for a close link between the thyroid hormone transport system and the aromatic amino acid transport system T in erythrocytes.
J Biol Chem. 1990 Oct 5;265(28):17000-4.
6
Novel cold-sensitive cytosolic 3,5,3'-triiodo-L-thyronine-binding proteins in human red blood cell. Isolation and characterization.人类红细胞中新型冷敏性胞质3,5,3'-三碘-L-甲状腺原氨酸结合蛋白。分离与鉴定。
J Biol Chem. 1991 Sep 5;266(25):16415-9.
7
Adsorption equilibria of thyroid hormones in the liver cell.肝细胞中甲状腺激素的吸附平衡
Eur J Biochem. 1977 Oct 17;80(1):25-33. doi: 10.1111/j.1432-1033.1977.tb11851.x.

人红细胞中冷敏感胞质3,3',5-三碘-L-甲状腺原氨酸结合蛋白的分子互变：冷、热和pH处理的影响

Molecular interconversion of cold-sensitive cytosolic 3,3',5-tri-iodo-L-thyronine-binding proteins from human erythrocytes: effect of cold, heat and pH treatments.

作者信息

Fanjul A N, Farías R N

机构信息

Departamento de Bioquímica de la Nutrición, Instituto Superior de Investigaciones Biológicas (CONICET-UNT), San Miguel de Tucumman, Argentina.

出版信息

Biochem J. 1993 Mar 1;290 ( Pt 2)(Pt 2):579-82. doi: 10.1042/bj2900579.

DOI:10.1042/bj2900579
PMID:8452548
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1132313/
Abstract

Cytosolic 3,3',5-tri-iodo-L-thyronine-binding proteins (CTBP I, II and IV species) from human red blood cells undergo rapid loss of activity at low temperatures. Cold treatment of CTBPs was accompanied by dissociation of the polymeric protein to the 60 kDa inactive monomer. Re-activation of the cold-inactivated CTBP IV by warming resulted in association of the monomer to the active polymeric form. A similar association-dissociation phenomenon was also obtained isothermically, though pH changes. We conclude that CTBP I and CTBP II are polymeric forms of CTBP IV.

摘要

人红细胞中的胞质3,3',5-三碘-L-甲状腺原氨酸结合蛋白（CTBP I、II和IV型）在低温下活性迅速丧失。CTBPs经冷处理后，聚合蛋白解离为60 kDa的无活性单体。通过升温使冷失活的CTBP IV重新激活，导致单体缔合为活性聚合形式。通过改变pH值，也能等温获得类似的缔合-解离现象。我们得出结论，CTBP I和CTBP II是CTBP IV的聚合形式。